Multiple Choice Questions in Biochemistry by Vidya Sagar

"Mcqs in Biochemistry" by G. Vidya Sagar
Netlibrary Inc | Edition : 2008 | ISBN: 8122426271 | 300 pages | PDF | 1 MB

Competitive Examinations are the order of the day. All Colleges conducting professional courses at PG level are admitting students based on common entrance examination, which is of objective type. In Pharmacy, M.Pharm admissions are based on qualifying the GATE enterance examination conducted by Govt. of India. In this book, The author has done good work in preparing several objective questions which help the students to face the subject in the examination with poise and confidence. The book is well balanced and consists of multiple choice questions from all the important topics like carbohydrate metabolism and other important Biochemical aspects. The typesetting and quality of printing is good. The author is also well experienced in taking up this type of work. I recommend this book to all the students preparing for GATE examination and also for Medical and Pharmacy College libraries.

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How to regulate UREA cycle in human body..?

The urea cycle operates only to eliminate excess nitrogen. On high-protein diets the carbon skeletons of the amino acids are oxidized for energy or stored as fat and glycogen, but the amino nitrogen must be excreted. To facilitate this process, enzymes of the urea cycle are controlled at the gene level. With long-term changes in the quantity of dietary protein, changes of 20-fold or greater in the concentration of cycle enzymes are observed. When dietary proteins increase significantly, enzyme concentrations rise. On return to a balanced diet, enzyme levels decline. Under conditions of starvation, enzyme levels rise as proteins are degraded and amino acid carbon skeletons are used to provide energy, thus increasing the quantity of nitrogen that must be excreted.

Short-term regulation of the cycle occurs principally at CPS-I, which is relatively inactive in the absence of its allosteric activator N-acetylglutamate. The steady-state concentration of N-acetylglutamate is set by the concentration of its components acetyl-CoA and glutamate and by arginine, which is a positive allosteric effector of N-acetylglutamate synthetase.

Fundamentals of Biochemistry: CD-ROM ~ Donald Voet, Pratt

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A virtual disc is needed to access the file. (MagicDisc, PowerISO, etc.) 

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Free Biochemistry Classes Online by Top Universities and Colleges

Top schools and universities offer free online coursework in various topics through a program called open courseware (OCW). First developed by Massachusetts Institute of Technology, the programs are the same as a paid course at a traditional college. A person does not earn college credit for the course.

Where Can I Find a Free Biochemistry Class Online?

Opencourseware was developed with the mission of sharing information and helping people improve their mind. Based on the principles of co-existence and co-prosperity, many countries around the world are following the guidelines originally conceived by Massachusetts Institute of Technology. Almost any topic of interest can be learned free of charge online, from French to biochemistry. The following schools have OCW programs for a person seeking training in biochemistry.

Massachusetts Institute of Technology

Massachusetts Institute of Technology offers a graduate level course in biochemistry. Lecture notes are provided on the major concepts of biochemistry, kinetics, the Chemical Kinetics Simulator 1.01, chemical thermodynamics, chemical equilibrium and mystery protein. The program focuses on the analytical methods used to dissect biological issues. Students study the structure of proteins in the regulatory, catalytic and binding stages.

The University of Arizona

The University of Arizona offers The Biochemistry Project, which consists of several free biochemistry courses online. Students review the basics of biochemistry, including molecules, amino acids, the clinical correlates of pH levels, acids and bases, enzymes and catalysts energy and metabolism. The courses provide multiple problem sets, or tests, for students to assess how well they know the presented material.

The University of Arizona has recently expanded its offerings to include chemistry of amino acids. Other OCW courses are cell biology, immunology, Mendelian genetics and molecular biology.

University of Akron

The University of Akron offers an overview of concepts in biochemistry that covers different areas of biochemistry, including alpha helix protein, acetyl co-enzyme A, amylase, beta sheet protein, collagen, hammerhead ribozyme, heme and FAD. An interesting feature of the site is an interactive collection of animated files that display molecules being rotated so students can observe their geometry. The site includes a chemical database and a periodic table of elements.

Texas A&M University

The biochemistry course at Texas A&M University offers students lecture notes to present material that is similar to what would be learned in a traditional lecture course. The topics covered in class and through the lecture notes include bioenergetics, introductions to metabolism, glycolysis, pentose phosphate pathway, biological reduction-oxidation reaction (redox) reactions, glycogen metabolism and the citric acid cycle.

Related articles to Biochemistry Online Class

• Learn Biochemistry Online: Overview of Biochemistry Study Options

  Online Biochemistry programs vary widely in both scope and type. Some biochemistry programs are simple learn-at-your-own-pace courses that end with no certification or credentials. Others are undergraduate- or graduate-level college degrees set on traditional class schedules.

• Schools with Bachelor Degrees in Biochemistry

  Biochemistry combines the studies of biology, chemistry and physics to research how science affects living organisms. Students interested in becoming researchers, physicians or scientists may benefit from schools with advanced facilities and an accomplished faculty. Biochemistry students may find student-sponsored science organizations or affiliated national biochemistry associations offer career and research events which may intensify an academic experience.

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Carbohydrates: The Essential Molecules of Life

This book provides the "nuts and bolts" background for a successful study of carbohydrates - the essential molecules that not only give you energy, but are an integral part of many biological processes.

A question often asked is 'Why do carbohydrate chemistry?' The answer is simple: It is fundamental to a study of biology. Carbohydrates are the building blocks of life and enable biological processes to take place.

Therefore the book will provide a taste for the subject of glycobiology. Covering the basics of carbohydrates and then the chemistry and reactions of carbohydrates this book will enable a chemist to gain essential knowledge that will enable them to move smoothly into the worlds of biochemistry, molecular biology and cell biology.

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Principles and Techniques of Biochemistry and Molecular Biology

Principles and Techniques of Biochemistry and Molecular Biology By Keith Wilson, John Walker

Publisher: Cam.bridg.e Univers.ity Pr.ess 2010 | 760 Pages | ISBN: 0521516358 , 0521731674 | File type: PDF | 9 MB

Description about the Book:
This best-selling undergraduate textbook provides an introduction to key experimental techniques from across the biosciences. It uniquely integrates the theories and practices that drive the fields of biology and medicine, comprehensively covering both the methods students will encounter in lab classes and those that underpin recent advances and discoveries. Its problem-solving approach continues with worked examples that set a challenge and then show students how the challenge is met. New to this edition are case studies, for example, that illustrate the relevance of the principles and techniques to the diagnosis and treatment of individual patients. Coverage is expanded to include a section on stem cells, chapters on immunochemical techniques and spectroscopy techniques, and additional chapters on drug discovery and development, and clinical biochemistry. Experimental design and the statistical analysis of data are emphasised throughout to ensure students are equipped to successfully plan their own experiments and examine the results obtained.

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Enzyme Linked ImmunoSorbant Assay (ELISA)

Enzyme immunoassay combine the specificity of antibodies with the sensitivity of simple spectrophotometric enzyme assays by using antibodies or antigens coupled to an easily assayed enzyme that also possesses a high turnover number. ELISA is replacing RIA, despite the latter already being established, extensively automated and sometimes more sensitive.

ELISA may be used for assaying antigens by either a competitive or a double antibody method and for assaying a specific antibody by an indirect method. All these methods require the preparation of a calibration curve during the assay.

The ELISA divided into three types, they are

a) Competitive method b) Double-antibody method c) Indirect method

a) Competitive method: A mixture of a known amount of enzyme - labelled antigen and an unknown amount of unlabelled antigen is allowed to react with a specific antibody to attach to a solid phase. After the complex has been washed with buffer, the enzyme substrate is added and the enzyme activity measured. The difference between this value and that of a simple lacking unlabelled antigen is a measure of the concentration of unlabelled antigen.

Major disadvantage: this method is that each antigen may require a different method to couple it to the enzyme; this is not so for the double-antibody method.

b) Double-antibody method: The unknown antigen solution is reacted with specific antibody attached to a solid phase, washed and treated with enzyme labelled antibody (directed against a different epitope, if monoclonal antibodies). After a further wash the enzyme substrate is added. The amount of enzyme activity measured under standard conditions directly proportional to the amount of antigen present. Advantage: It is that only one procedure required coupling the enzyme to all preparations.

c) Indirect method: The method may be used to measure antibody levels. The putative antiserum is reacted with specific antigen attached to a solid phase. Any specific antibody molecules bind to the antigen and all other material is washed away. Exposure of the complex to enzyme labelled anti-immunoglobulin antibody results in binding to any specific antibody molecules adsorbed from the original serum. The complex is washed and the substrate for the enzyme added, resulting in activity proportional to the amount of specific antibody in the serum.

 

ELISA, in which enzyme labelled antibody binds an antigen, leading to substrate breakdown and colour change, can be used to detect primary antigen-antibody reactions

ELISA uses an enzyme for labelling rattier than a radioisotope. Like the radioisotopes, the enzyme is covalently coupled to the antibody, in principle, this is the only difference between ELISA and RIA. ELISA measures bound enzyme activity rather than bound counts per minutes. Quantification requires measuring the colour intensity of the colored products generated by the enzyme and added substrate. The intensity of the colour is equivalent to the amount of labeled antibody bound to antigen. ELISA has replaced RIA in many clinical and basic science laboratories. RIAs are potentially hazardous and tedious, require bookkeeping, and involve radioisotopes. These reasons combined with the commercial availability of plate readers that can be measure the absorbance of 96 wells in less than a minute, account for ELISA's growing popularity. ELISA and RIA are similar in sensitivity. Theoretically, ELISA can be more sensitive than RIA because each enzyme molecule can generate hundreds of thousands of colored product molecules that can be measured. In contrast, ^12S I molecule decays only once. Once application of ELISA is to detect the presence and titre of specific antibody for the AIDS virus.

Applications of ELISA:

• Whilst ELISA can be used for the assay of virtually any antigen, hapten or antibody, it is used predominantly in clinical biochemistry laboratories to measure, for example, IgG, and IgE, oncofetal proteins, hematological factors, immune complexes and hormones such as insulin, oestrogen and human chorionic gonadotropin.
• Examples of its use in the study of infectious diseases include the detection of bacterial toxins, Candida albicans, rotaviruses, herpes simplex viruses and the hepatitis B surface antigen.
• ELISA has also been used extensively for the assay of antibodies in infectious diseases including: anti-viral antibodies, e.g. to Epstein-Barr virus and rubella virus; anti-bacterial antibodies, e.g. to Brucella, Rlckettsia and Salmonella species, anti-fungal antibodies, e.g. to Aspergillus and Candida species, anti-parasite antibodies, e.g. to Plasmodium, Schistosoma and Trypanosoma species, and autoantibodies, e.g. anti-DMA and anti thyroglobulin.

monoclonal antibodies

When an antigen is introduced into the circulatory system of a higher vertebrate, it stimulates specific B-lymphocytes to produce antibodies. The antibodies are the immunoglobulins and they circulate in the blood serum.

When the immune system of an animal encounters a new antigen, it responds to specific antigenic determinants called 'epitopes' located on the antigen. Thus, a protein antigen may possess several epitopes and would induce the formation of several different antibodies, each specific for one epitope. Such a polyclonal antibody response facilitates the localization, phagocytosis and complement-mediated lysis of antigens.

For most reasearch, diagnostic and therapeutic purposes, "Monoclonal antibodies", derived from a single clone and thus specific for a single epitope are preferable.

In 1975, "Georges Kohler" and "cesar Milstein" devised a method for preparing monoclonal antibody, which quickly became one of the immunology's key technologies. These work got Nobel Prize in 1984.

Basic concept Principle on the monoclonal antibodies production:

By fusing a normal activated, antibody producing B-cell with a myeloma cell(a cancerous plasma cell), they were able to generate a hybrid cell, called a 'hybdridoma', that possessed the immortal-growth properties of the myeloma cell and secreted the antibodies produced by the B-cell. The resulting clones of hybridoma cells,which secrete large quantities of monoclonal antibodies can be cultured indefinitely. The development of techniques for producing monoclonal antibody gave immunologists a powerful and versatile research tool.

Production &Selection of hybridoma cells:

One common method requires the use of myeloma cells that are deficient (because of previously selected mutation) for one of the nucleotide salvage pathways, making them unable to grow in HAT medium (named for its three components -Hypoxanthine, Aminopterin, and Thymidine). If the mixture of hybridomas and unfused parental cells is placed in this medium, the parental myeloma cells can not survive. The B-cell X myeloma cells can survive because the B-cell contributes the missing enzyme for the salvage pathway. Although unfused B-cells are able to survive in HAT medium, these cells do not live for extended periods in vitro and thus die out.

HAT selection depends on the fact that mammalian cells can synthesize nucleotides by two different pathways; the denovo and the salvage pathways. The denovo path way, in which a methyl or formyl group is transferred from an activated form of tetrahydrofolate, is blocked by Aminopterin, a folic acid analogue. When the denovo path way is blocked, cells utilize the salvage pathway, which bypasses the aminopterin block by converting purines and pyrimidines directly intoYiucleotides for synthesis of DNA and RNA. The enzymes catalyzing the salvage pathway include Hypoxanthine-Guanine Phosphoribosyl transferase(HGPRT) and Thymidine kinase(TK). A mutation in either of these two enzymes blocks the ability of the cell to use the salvage pathway. HAT medium contains aminopterin to block the denovo pathway and hypoxanthine and thymidine to allow growth by the salvage pathway. Therefore, cells that lack either HGPRT or TK will die in HAT medium, because they lake the ability to use the salvage pathway to acquire essential intermediates for the synthesis of nucleic acids.

In hybridoma technology, the myeloma cells are actually double mutants. As mentioned above, they lack the enzyme HGPRTase and therefore are deselected in HAT. They have lost the ability to produce immunoglobulins (Ig- mutants).

Applications of Monoclonal Antibodies:

1. Improved diagnostic reagents: For the assay of wide range of compounds, including hormones, antibiotic interferons, and blood-clotting factors, antibody-antigen reactions are widely used. For blood typing and diagnostic microbiology, the ability of antibodies to agglutinate or precipitate cells have been used; the homogeneity of Monoclonal antibodies reduces reaction times and the likelihood of non-specific cross-reactions between the antibody and antigen is lessened by the use of Monoclonal antibodies. It is possible to diagnose pregnancy or ovulation more precisely with the Monoclonal antibodies.

2.Protein purification: Monoclonal antibody affinity columns are prepared by coupling monoclonal antibodies to a cyanogen bromide-activated chromatography matrix, for example, sepharose. Monoclonal antibodies immomabalized in this way are particularly valuable for the purification of proteins. Since the monoclonal antibodies has a unique specificity for the desired proteins, the level of contamination by unwanted proteins, usually, is very low. Even when the concentrating of the desired protein, in a mixture of proteins, is very low, Monoclonal antibodies has the capacity to combine with it and to remove the whole of it. For example, when the concentration of interferon was less than 0.02%, the anti-interferon monoclonal antibodies enable the recovery of 97% of the interferon by immunoaffinity chromatography.

3.Improved sensitivity and reproducibility of existing immunoassays or new assays for

Histocompatibility antigens, Complement component, Human growth hormones, Interkeukins, Oestrogen, Blood clotting factors, Sperm antigens, Blood group antigens, Progesterone, Fibronectin, Interferons, Gastrin

4. Therapy:

• Correction of drug over dose
• Reduction of risks associated with bone marrow transplants
• Detection of tumour metastases
• Treatment of cancer (directly, or by targeting “cytotoxic drugs”.

5. Diagnosis of:

• Sexually Transmitted Diseases (STDs)
• Cancer(by detection of Onco -foetal antigens)

Few Questions from Immunology

1.Detoxification converts ______ substances formed in the body into _____________ substances which are easily excreted out by the excretory routes.

a) Non-toxic, toxic b) Toxic, Non-toxic c) Carbohydrates to Amino acids

d) Protein to non-protein

2. __________ and ______ form Hippuric acid

a) Benzene + Glycine b) Benzoic acid + Alanine c) Glycine + Benzoic acid d) Banzaldehyde and glycine

3. The lymphocytes are the primary cell for ________ system

a) Respiratory b) Excretory c) Immune d) Digestive

4. The T-lymphocytes are ______ derived

a) Thyroid b) Tumor c) Thymus d) None of the above

5. B-Lymphocytes are responsible for _______ immunity

a) Humoral ; antigen b) Humoral : Antibody c) Cell mediated and antigen d) Cell mediated and antibody

6. Identify the organ which shows first line defense in ______

a) Cellular factors ; innate b) Mucous membrane; Acquired c) Skin; Innate d) Macrophages; Innate

7. Identify the largest organ in human system

a) Mucus membrane b) Liver c) Kidney d) Skin

8. Identify the systems which are examples to signal transduction mechanisms

a) Blood coagulation                            b) Complement system                                          c) Hormonal mechanism                    d) All of the above

9. Interferon's are ……..

a) Interferes in bacterial infection b) It interferes to block the viral life cycle in viral infection

c) These are a group of soluble non-toxic glycoproteins d) both ‘b’ and ‘c’

10. Phagocytic cells are discovered by

a) Louis paster                              

b) Adwardjenner                                                                       

c) Mitchincoff      

d) Rodney porter

11. Professional phagocytes are ……..

a) Eosinophylls b) Neutrophiles c) Macrophages d) Basophiles

12. Immunity means…

a) The resistance developed by man during his life

b) The resistance shown by the most against the invaginated microbes and their products

c) All of the above                 d) None of the above

13. Temperature is one of the physiological barrier, which functions…..

a) Normal body temperature inhibits growth of some pathogens

b) Fever responsible to inhibits growth of some pathogens

c) all of the above                         d) none of the above

14. Lysozyme is ____, which inhibits

a) an enzyme, viral life cycle    b) an enzyme, bacterial cell wall synthesis

c) a hormone, viral life cycle   d) a hormone, bacterial cell wall synthesis

15. transfer of immunity from immunized host to non-immunized host is called as …

a) Natural active immunity                        b) Artificial active immunity

c) Natural passive immunity          d) Artificial passive immunity

Protein Structure & Function

Proteins are an important class of biological macromolecules present in all organisms. All proteins are polymers of amino acids. Classified by their physical size, proteins are nanoparticles (definition: 1-100 nm). Each protein polymer – also known as a polypeptide – consists of a sequence of 20 different L-α-amino acids, also referred to as residues. For chains under 40 residues the term peptide is frequently used instead of protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations, driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van Der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, and dual polarisation interferometry to determine the structure of proteins.

Protein structures range in size from tens to several thousand residues Very large aggregates can be formed from protein subunits: for example, many thousand actin molecules assemble into a microfilament.

A protein may undergo reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different conformations, and transitions between them are called conformational changes.

 

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Combination vaccines with whole cell pertussis

While pertussis was thought to have been eradicated entirely from the United States, in recent years the disease has made a comeback and resulted in fatalities. At the same time, many parents have declined to vaccinate their children against the disease for fear of side effects;  however, most side effects of the vaccination are moderate and severe problems closely following DPT immunization happen very rarely. These include a serious allergic reaction, prolonged seizures, a decrease in consciousness, lasting brain disease, or death. A study published in the journal Pediatrics in 2009 concluded that the largest risk among unvaccinated children is the disease the vaccination is designed to protect against.

British research in the 1980s into whole-cell DTP, which is now rarely available in developed countries, suggested that such severe neurologic events occur after approximately 1 in 140,000 doses of the DPT vaccine (0.0007%). Most of the reactions to whole-cell DPT injection are thought to be from the pertussis component.

In 1994, the Institute of Medicine of the US National Academy of Sciences published a report stating that if the first symptoms of neurological damage occurred within the first seven days following vaccination with whole-cell pertussis vaccine, the evidence was compatible with the possibility that it could be the cause of permanent brain damage in otherwise apparently healthy children. It continued by stating. DTP vaccination has different pros & cons depending on the nature, place, and surrounding.

This serious acute neurologic response to whole-cell DPT is a rare event. The estimated excess risk ranged from 0 to 10.5 per million immunizations (IOM, 1991). The committee stresses that this is not the strongest statement regarding causality; the evidence does not "establish" or "prove" a causal relation....

The evidence remains insufficient to indicate the presence or absence of a causal relation between DPT and chronic nervous system dysfunction under any other circumstances. That is, because the NCES is the only systematic study of chronic nervous system dysfunctions after DPT, the committee can only comment on the causal relation between DPT and those chronic nervous system dysfunctions under the conditions studied by the NCES. In particular, the chronic dysfunctions associated with DPT followed a serious acute neurologic illness that occurred in children within 7 days after receiving DPT.

Moderate reactions to DTP vaccines occur in 0.1% to 1.0% of children and include ongoing crying (for three hours or more), a high fever (up to 40 °C / 105 °F), and an unusual, high-pitched crying.

Since 2002, whole-cell pertussis vaccines are no longer used in the US.

(source: wikipedia)

What is the Triple Antigen Vaccine?

 Triple Antigen vaccine is a combination of Diphtheria, Tetanus, and Pertussis. The vaccine stimulates the production of antibodies to immunize the body against the causative agents of the three viruses listed below.

 

'DPT' (also DTP and DTwP) refers to a class of combination vaccines against three infectious diseases in humans: diphtheria, pertussis (whooping cough) and tetanus. The vaccine components include diphtheria and tetanus toxoids, and killed whole cells of the organism that causes pertussis (wP).

DTaP (also known as Tdap,DTPa, and TDaP) refers to similar combination vaccines in which the pertussis component is acellular.

Also available is the DT or TD vaccine, which lacks the pertussis component.

In the Netherlands, the acronym DTP refers to a combination vaccine against diphtheria, tetanus, and poliomyelitis. There, pertussis is known as kinkhoest and DKTP refers to a combination vaccine against diphtheria, pertussis/kinkhoest, tetanus, and polio.

The usual course of childhood immunization is five doses between 2 months and 15 years. For adults, separate combination vaccines are used that adjust the relative concentrations of their components.

Question from Examinations:

Triple antigen is not given for

(1) Tetanus

(2) Diphtheria

(3) Whooping cough

(4) Typhoid (this is Answer)

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Combination vaccines with whole cell pertussis

Biology Complete Book Collection

 

 

Booklist

Anatomy and Physiology :

Anatomia Color Atlas and Textbook of Human Anatomy Volume 3 2003 Thieme
Anatomy of the Human Body – Henry Gray
Atlas Of Human Skeletal Anatomy – Juraj Artner
Color Atlas and Textbook of Human Anatomy ,Volume I Locomotor System – Werner Platzer, Werner Kahle, M. Frotscher
Color Atlas and Textbook of Human Anatomy, Volume 2 Internal Organs – Werner Platzer, Werner Kahle, M. Frotscher
Color Atlas Of Cytology, Histology, And Microscopic Anatomy – Wolfgang Kuhnel
Color Atlas of Physiology 5th Ed. – A. Despopoulos
Color Atlas of Ultrasound Anatomy – Berthold, M.D. Block
Human Anatomy 6th ed – Kent Van De Graaff
Human Physiology – The Mechanisms of Body Function 8th ed – Vander
Pocket Atlas of Human Anatomy Based on the International Nomenclature – Heinz Feneis, Wolfgang Dauber
Pocket Atlas Of Radiographic Anatomy 2d ed – Torsten B. Moller, Emil Reif
Review of Medical Physiology – 21 Edition – William F. Ganong
Schaum’s Outline of Human Anatomy and Physiology – Kent M. Van De Graaff, R. Ward Rhees
Understanding Human Anatomy and Physiology – Sylvia S. Mader

Neuroanatomy :
Atlas of Neuroanatomy and Neurophysiology – Frank H. Netter
Color Atlas of Neuroscience Neuroanatomy and Neurophysiology – Ben Greenstein, Adam Greenstein
High-Yield Neuroanatomy – James D. Fix
Neuroanatomy An Atlas of Structures, Sections, and Systems – Duane E. Haines

Anthropology :
A Handbook Of Economic Anthropology – James G. Carrier
Biological Anthropology An Evolutionary Perspective – Barbara J King
Genetic NatureCulture Anthropology and Science beyond the Two-Culture Divide – Alan Goodman

Behavioral science :
International Encyclopedia Of The Social & Behavioral Sciences
Methods of Behavior Analysis in Neuroscience – Jerry J. Buccafusco

Biochemistry :
An Introduction to Computational Biochemistry – Jeremy J. Ramsden
Analytical Biochemistry 3rd ed – David Holme, Hazel Peck
Basic Concepts in Biochemistry A Student’s Survival Guide 2d ed – Hiram F. Gilbert
Biochemistry 3 ed – Lippincott
Biochemistry 5th ed – Jeremy M. Berg, John L. Tymoczko, Lubert Stryer
Biochemistry of Lipids, Lipoproteins and Membranes, 4th edition – .E. Vance, J.E. Vance
Biochemistry of Signal Transduction and Regulation 3d ed – Gerhard Krauss
Biochemistry The Chemical Reactions Of Living Cells 2d Ed Vols 1&2 – David E. Metzler
Biochemistry The Molecular Basis of Life – Trudy McKee, James R McKee
Color Atlas Of Biochemistry 2d ed – Jan Koolman, Klaus-Heinrich Rohm
Encyclopedia of Physical Science and Technology – Biochemistry – 3rd Ed
Flavonoids – Andersen, Markham
Harper’s Illustrated Biochemistry – Robert K. Murray, Darryl K. Granner, Peter A. Mayes, Victor W. Rodwell
Inorganic Biochemistry of Iron Metabolism From Molecular Mechanisms to Clinical Consequences, 2nd Edition – Robert R. Crichton
Lehninger Principles of Biochemistry, Fourth Edition – David L. Nelson, Michael M. Cox
Marks� Basic Medical Biochemistry A Clinical Approach, 2nd Edition – Colleen Smith
Modern Experimental Biochemistry 3d ed – Rodney F. Boyer
Toxicological Chemistry and Biochemistry, Third Edition – Stanley E. Manahan

Bioethics :
Encyclopedia of Bioethics, 3rd edition – Stephen G. Post
Genetics and human behaviour the ethical context – Nuffield Council
Is Human Nature Obsolete Genetics, Bioengineering, and the Future of the Human Condition.(Book review) An article from Theological Studies – Andrew Lustig

Bioinformatics :
An Introduction to Genetic Algorithms – Melanie Mitchell
Artificial Intelligence and Molecular Biology – Lawrence Hunter
Beginning Perl for Bioinformatics – James Tisdall
Bioinformatics – From Genomes to Drugs – Thomas Langauer
Bioinformatics A Practical Guide to the Analysis of Genes and Proteins – Andreas D. Baxevanis , B. F. Francis Ouellette
Bioinformatics Computing – Bryan Bergeron
Bioinformatics Methods and Protocols Methods in Molecular Biology – Stephen Misener , Stephen A., Krawetz
Bioinformatics Sequence and Genome Analysis – David W. Mount
Bioinformatics The Machine Learning Approach, Second Edition – Pierre Baldi, Soren Brunak
Blast – Ian Korf, Mark Yandell, Joseph Bedell
Calculating the Secrets of Life Applications of the Mathematical Sciences in Molecular Biology – Eric S. Lander, Michael S. Waterman
Computational Cell Biology – Christopher Fall, Eric Marland, John Wagner, John Tyson
Computational Molecular Biology An Algorithmic Approach – Pavel A. Pevzner
Computational Molecular Biology An Introduction – Peter Clote, Rolf Backofen
Current Topics in Computational Molecular Biology – Tao Jiang , Ying Xu , Michael Q. Zhang
Data Analysis and Visualization in Genomics and Proteomics – Francisco Azuaje
Data Mining Multimedia, Soft Computing, and Bioinformatics – Sushmita Mitra, Tinku Acharya
Developing Bioinformatics Computer Skills – Cynthia Gibas, Per Jambeck
Gene Regulation and Metabolism Post-Genomic Computational Approaches – Julio Collado-Vides
Genetic Programming On the Programming of Computers by Means of Natural Selection – John R. Koza
Introduction to Bioinformatics – Arthur M. Lesk
Introduction to Computational molecular biology – Carlos Setubal, Joao Meidanis
Mastering Perl for Bioinformatics – James D. Tisdall
Microarrays for an Integrative Genomics Computational Molecular Biology – Isaac S. Kohane, Alvin Kho, Atul J. Butte
Practical Genetic Algorithms – Randy L. Haupt, Sue Ellen Haupt
Sequence Analysis In A Nutshell – Darryl Leon, Scott Markel

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Biological Psychiatry :
Psychiatry as a Neuroscience – Mario Maj
Textbook of Biological Psychiatry – Jaak Panksepp

Biophysics :
An Introduction To Environmental Biophysics – Gaylon S. Campbell, John M. Norman
Biophysics – Vasantha Pattabhi, N. Gautham
biophysics 4th ed – oland Glazer
Computational Biochemistry and Biophysics – Oren M. Becker
Lectures in Theoretical Biophysics – K. Schulten , I. Kosztin

Biotechnology :
Biological Nanostructures and Applications of Nanostructures in Biology Electrical, Mechanical, and Optical Properties – Michael Stroscio
Bionanotechnology Lessons from Nature – David S. Goodsell
Biotech Industry – A Global, Economic and Financing Overview – B Bergeron & P Chan
Biotechnology and Communication The Meta-Technologies of Information – Sandra Braman
Biotechnology for Waste and Wastewater Treatment – Nicholas P. Cheremisinoff
Biotechnology Unzipped Promises And Realities – Eric S. Grace
Carbohydrate Biotechnology Protocols – Christopher Bucke
Cell and Tissue Culture Laboratory Procedures – Alan Doyle
Cereal Biotechnology – Peter C. Morris , James H. Bryce
Environmental Biotechnology Principles and Applications – Bruce E. Rittmann, Perry L. McCarty
From Biotechnology to Genomes The Meaning of the Double Helix – Philippe Goujon
Fruit and Vegetable Biotechnology – Victoriano Valpuesta
Glossary of Biotechnology Terms, Third Edition – Kimball Nill
History and Trends in Bioprocessing and Biotransformation – T. Scheper, N. N. Dutta, F. Hammar
History of Modern Biotechnology I – Springer
History Of Modern Biotechnology II – Springer
Industrial Pharmaceutical Biotechnology – Heinrich Klefenz
Marine Biotechnology in the 21st Century – Nrc
Modern Advances in Chromatography – Springer
Physics And Chemistry Basis Of Biotechnology – De Cuyper & Bulte
Plant Biotechnology and Transgenic Plants – Kirsi-Marja Oksman-Caldentey , Wolfgang H. Barz
Separation Processes In The Food & Biotechnology Industries – GRANDISON
Synthetic Polymers for Biotechnology and Medicine – Ruth Freitag
The Application of Biotechnology to Industrial Sustainability – Christian Aagaard Hansen
The Biotechnology of Ethanol – M Roher
Understanding Biotechnology – Aluizio Borem, Fabricio R. Santos, David E. Bowen

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botany :
Aquarium Plants Their Identification Cultivation and Ecology – Karel Rataj
Carnivorous plants of the world – James Pietropaolo
Green Plants Their Origin and Diversity – Peter R. Bell, Alan R. Hemsley
Handbook of Plant & Crop Physiology Revised & Expanded – Mohammad Pessarakli
Introduction to Botany – James Schooley

Cell and Molecular Biology :
Advanced Molecular Biology A Concise Reference – Richard M. Twyman
Basic Cell Culture Protocols Methods in Molecular Biology – Cheryl D. Helgason, Cindy L. Miller
Cell Biology A Short Course 2d ed – Stephen R. Bolsover, Jeremy S. Hyams
Cell Cycle Control Mechanisms and Protocols Methods in Molecular Biology – Tim Humphrey, Gavin Brooks
Cellular Biology, A Short Course 2Ed – Stephen R. Bolsover
Chiral Separations Methods and Protocols – Gerald Gubitz
Data Analysis in Molecular Biology and Evolution – Xuhua Xia
Dictionary Of Biochemistry And Molecular Biology 2d ed – J. STENESH
DNA�Protein Interactions Principles and Protocols Second Edition – Tom Moss
Embryonic Stem Cells, Methods And Protocols – Kursad Turksen
Flow Cytometry Protocols 2d ed – Teresa S. Hawley
Genomic Imprinting – Andrew Ward
High-Yield Cell and Molecular Biology – Ronald W Dudek
Histology and Cell Biology – Abraham Kierszenbaum
Membrane Protein Protocols – Barry S. Selinsky
Molecular Analysis Of Cancer – Carrie Fidler
Molecular and Cellular Biology of Neuroprotection in the CNS – Christian Alzheimer
Molecular Biology in Cellular Pathology – John Crocker , Paul G. Murray
Molecular Biology in Medicinal Chemistry – D. Steinhilber
Molecular Biology of Human Cancers An Advanced Student’s Textbook – Wolfgang A. Schulz
Molecular Biology of the Gene, Fifth Edition – James D. Watson
Molecular Biology of the Parathyroid – Tally Naveh-Many
Molecular Cell Biology 5th ed – Lodish et al
Nuclear Import and Export in Plants and Animals – T. Tzfira, Vitaly Citovsky
Oxford Dictionary Of Biochemistry And Molecular Biology – Teresa Atwood
Pcr Cloning Protocols – Harry W. Janes, Bing-Yuan Chen
PCR Protocols 2d ed – John M. S. Bartlett
Plant Cell Biology – William V. Dashek
Protein Expression A Practical Approach – B. D. Hames
Protein Structure Prediction, methods and protocol – David M. Webster
Rt-Pcr Protocols – Joe O�Connell
Schaum’s Easy Outline Molecular and Cell Biology – William Stansfield, Raul J Cano, jaime S. Colome
Single Nucleotide Polymorphisms – Pui-Yan Kwok
Stem Cell Biology – Daniel R. Marshak
Stem Cell Biology and Gene Therapy – Peter J. Quesenberry
Steroid Receptor Methods – Benjamin A. Lieberman
The Biogenesis Of Cellular Organelles – Chris Mullins
The Encyclopedia Of Molecular Biology – Creighton
TWO-HYBRID SYSTEMS – Paul N. MacDonald

 

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Developmental biology :
Developmental Biology – Scott F. Gilbert
developmental biology protocols – Rocky S. Tuan and Cecilia W. Lo
Evolutionary Developmental Biology of the Cerebral Cortex – Novartis Foundation
Key Experiments in Practical Developmental Biology – Jennifer Knight

Ecology :
Ecology of the Planted Aquarium A Practical Manual and Scientific Treatise for the Home Aquarist, Second Edition – Diana Walstad
The Nature Of Design Ecology Culture – Oxford University Press
Plant Ecology – Erwin Beck
Research Techniques in Animal Ecology – Luigi Boitani
The Ecology of the Cambrian Radiation – Andrey Zhuravlev

Entomology :
Entomology 3rd ed – C.Gillott

Epidemiology :
Basic Epidemiology – Beaglehole , Bonita

Evolution :
Cooperation in Primates and Humans Mechanisms and Evolution – Peter M. Kappeler
Human Evolution – An Illustrated Introduction, 5th Edition – Roger Lewin
Molecular population genetics and evolution – Masatoshi Nei
Selective Sweep – Dmitry Nurminsky
The Phenomenon of Science A cybernetic approach to human evolution – Turchin V.F

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General :
Biology 6th ed – Raven Johnson
Biology 7th ed – Campbell, Reece
Biology Macmillan Science Library – Richard Robinson
Biology Science for Life – Colleen Belk, Virginia Borden
Discover Biology 2nd edition – Cain, Michael
Life The Science of Biology 7th ed – Bill Purves, David Sadava
Modern Biology – Postlethwait , Hopson
Practical approach to microarray data analysis – Daniel P. Berrar, Werner Dubitzky, Martin Granzow
Schaum’s Outline of Biology – Fried, George H.
The New Penguin Dictionary Of Biology – M. Abercrombie

Genetics :
ABC of Clinical Genetics – Helen M. Kingston
Color Atlas of Genetics, 2nd ed – Eberhard Passarge
Evolutionary Genetics 2d ed – MAYNARD SMITH
Functional Genomics – Michael J. Brownstein , Arkady B. Khodursky
Genetics A Conceptual Approach – Pierce, B. A
Genetics and the Logic of Evolution – Kenneth M. Weiss
Genetics Principles And Analysis – Daniel L. Hartl
Genetics Vol 1, A-D – Macmillan Science Library
Genetics Vol 2, E-I – Macmillan Science Library
Genetics Vol 3, K-P – Macmillan Science Library
Genetics Vol 4, R-Z – Macmillan Science Library
Genome The Autobiography of a Species in 23 Chapters – Matt Ridley
Genomics and Proteomics Functional and Computational Aspects – S?ndor Suhai
Genomics Protocols – Michael P. Starkey , Ramnath Elaswarapu
Introduction To Molecular Genetics And Geonomics – hearts
Introduction to Proteomics Tools for the New Biology – Daniel C. Liebler
Modern Microbial Genetics 2d ed – Uldis N. Streips
Plant Genomics and Proteomics – Christopher A. Cullis
Population Genetics A Concise Guide – John H. Gillespie
Protein Arrays, Biochips, and Proteomics – Joanna S. Albala
Proteomics in Practice – A Laboratory Manual of Proteome Analysis – Tom Naven
Schaum’s Outline of Theory and Problems of Genetics – William D. Stansfield
The Behavioral Genetics of Psychopathology A Clinical Guide – Kerry L. Jang
The Genetics and Biology of Sex Determination – Novartis Foundation
The Genomics Age How DNA Technology Is Transforming the Way We Live and Who We Are – Gina Smith

 

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Histology :
High-Yield Histology 2d ed – Ronald W Dudek

Mathematical Biology :
Algebraic Statistics for Computational Biology – Lior Pachter and Bernd Sturmfels
Mathematical Biology I. An Introduction Third Edition – J.D. Murray
Tutorials in Mathematical Biosciences – M. Morel, Cachan

Biostatistics :
Advances in Clinical Trial Biostatistics – Nancy L. Geller
Biostatistical Methods in Epidemiology – STEPHEN C. NEWMAN
Biostatistics A Methodology For the Health Sciences – Gerald van Belle, Patrick J. Heagerty, Lloyd D. Fisher, Thomas S. Lumley
High-Yield Biostatistics – A. Glaser
Introductory Biostatistics – Chap T. Le
Introductory Biostatistics for the Health Sciences Modern Applications Including Bootstrap – Michael R. Chernick, Robert H. Friis
Primer of Biostatistics 5th Ed – Stanton A. Glantz

MicroBiology :
Applied Dairy Microbiology, Second Edition – Elmer H. Marth
Benson’s Microbiological Applications Laboratory Manual in General Microbiology – Alfred E Brown
Freshwater Microbiology – Biodiversity And Dynamic Interactions Of Microorganisms In The Aquatic Environment – David Sigee
Kaplan Medical Step 1 Microbiology – Immunology
Laboratory Exercises in Microbiology – John P Harley, John Harley
Lippincott’s Illustrated Reviews Microbiology – William A Strohl
Microbiology Demystified – Tom Betsy, James Keogh
Modern Food Microbiology 6th ed – James M. Jay
The Microbiology of Anaerobic Digesters – Michael H. Gerardi
Wastewater Microbiology – Gabriel Bitton
Wastewater Pathogens – Michael H. Gerardi, Mel C. Zimmerman
World of Microbiology and Immunology Vol 1 (A-L) – K. Lee Lerner
World of Microbiology and Immunology Vol 2 (M-Z) – K. Lee Lerner

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Neuroscience :
Brain Facts A Primer on the Brain and Nervous System – The Society for Neuroscience
Elements of Molecular Neurobiology 3d ed – C. U. M. Smith
Neurological Foundations of Cognitive Neuroscience – Mark D’Esposito
Neuroscience 3ed – DALE PURVES
Theoretical Neuroscience Computational and Mathematical Modeling of Neural Systems – Peter Dayan, L. F. Abbott

Paleontology :
GEOLOGY AND VERTEBRATE PALEONTOLOGY OF THE EARLY PLIOCENE SITE OF KANAPOI,NORTHERN KENYA – JOHN M. HARRIS
History of geology and paleontology – Zittel K.A.

Systems Biology :
Foundations of Systems Biology – Hiroaki Kitano
System Modeling in Cell Biology From Concepts to Nuts and Bolts – Zoltan Szallasi, J?rg Stelling, Vipul Periwa
Systems biology – dynamic pathway modeling – Olaf Waulkenhour
Systems Biology Properties of Reconstructed Networks – Bernhard o. Palsson

Taxonomy :
Key to Soil Taxonomy – Soil Survey Staff

Zoology :
Curious Creatures in Zoology – John Ashton
Dictionary of Invertebrate Zoology
Integrated Principles of Zoology 11th ed – Hickman, Roberts, Larson
Zoology 5th ed – Miller , Harley

 

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Molecular Biology of the Cell, 5th Edition

Molecular Biology of the Cell, 5th Edition (with DVD)|Size : 1.86 GB

Hardcover: 1392 pages
Publisher: Garland Science
Language: English
ISBN-10: 0815341059
ISBN-13: 978-0815341055
Authors: Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter -

Includes DVD

 

Description: For nearly a quarter century Molecular Biology of the Cell has been the leading cell biology textbook. This tradition continues with the new Fifth Edition, which has been completely revised and updated to describe our current, rapidly advancing understanding of cell biology. To list but a few examples, a large amount of new material is presented on epigenetics; stem cells; RNAi; comparative genomics; the latest cancer therapies; apoptosis (now its own separate chapter); and cell cycle control and the mechanics of M phase (now integrated into one chapter).

The hallmark features of Molecular Biology of the Cell have been retained, such as its consistent and comprehensive art program, clear concept headings, and succinct section summaries. Additionally, in response to extensive feedback from readers, the Fifth Edition now includes several new features.

It is now more portable. Chapters 1-20 are printed and Chapters 21-25, covering multicellular systems, are provided as pdf files on the free Media DVD-ROM which accompanies the book.* And for the first time, Molecular Biology of the Cell now contains end-of-chapter questions. These problems, written by John Wilson and Tim Hunt, emphasize a quantitative approach and the art of reasoning from experiments, and they will help students review and extend their knowledge derived from reading the textbook.

The Media DVD-ROM, which is packaged with every copy of the book, contains PowerPoint presentations with all of the figures, tables and micrographs from the text (available as JPEGs too). Also included is the Media Player, which plays over 125 movies and animations, videos, and molecular models all with voice-over narration. A new reader-friendly feature is the integration of media codes throughout the text that link directly to relevant videos and animations. The Media DVD-ROM holds the multicellular systems chapters (21-25) of the text as well.

By skilfully extracting the fundamental concepts from this enormous and ever-growing field, the authors tell the story of cell biology, and thereby create a coherent framework through which readers may approach and enjoy this subject that is so central to all of biology.

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Download links to Biology ebook collections

Biology Complete Book Collection

The Index of the catalogues is given in the following link

Catalogue of the ebook (link)

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You can also download Babylon

Amino acid structure and properties online quiz

BRUSH BACK YOUR BASICS

Check out this online quiz on the structure, chemical nature, 3-letter and the 1-letter codes of the amino acids:

Amino acid Online quiz
(Just click on the above link)

Be sure that you are also able to draw the amino acids themselves and as part of a polypeptide chain.

Harper's Illustrated Biochemistry, 28th Edition

 

Harper's Illustrated Biochemistry,       28th Edition
Publisher: McGraw-Hill Medical 2009 | 704 Pages | ISBN: 0071625917 | CHM | 22 MB

Description:
Comprehensive, concise, and up-to-date, Harper's is unrivalled in its ability to clarify the link between biochemistry and the molecular basis of health and disease.The Twenty-Eighth Edition has undergone sweeping changes -- including a conversion to full-colour artwork and the substantial revision and updating of every chapter -- all to reflect the latest advances in knowledge and technology and to make the text as up-to-date and clinically relevant as possible.

Combining outstanding full-colour illustrations with integrated coverage of biochemical diseases and clinical information, Harper's Illustrated Biochemistry offers an organization and clarity not found in any other text on the subject.

NEW to this edition:

• Full-color presentation, including 600+ illustrations
• Every chapter opens with a Summary of the Biomedical Importance and concludes with a Summary reviewing the topics covered
• Two all-new chapters: "Free Radicals and Antioxidant Nutrients" and "Biochemical Case Histories" which offers an extensive presentation of 16 clinical conditions
• A new appendix containing basic clinical laboratory results and an updated one with a list of important websites and online journals
• NEW or updated coverage of important topics including the Human Genome Project and computer-aided drug delivery

 

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How to Study for Success

How to Study for Success

Jossey-Bass (2004-08-11) |               ISBN 0471431559 | 120 Pages | PDF | 8.7 MB

Description:

Develop powerful study skills that will last a lifetime!

When you have strong study habits, you learn more in class, get more out of your homework, and, best of all, have a much easier time completing any type of assignment. How to Study for Success lets you build those habits and master essential study skills that will help you become a better student.

Filled with easy-to-follow advice, this hands-on guide includes 7 Keys to Success that will help you improve your school performance:
* Get Ready to Study Now
* Get Organized
* Make the Most of Class Time
* Make the Most of Home Study Time
* Make the Most of Homework
* Put Your Computer to Good Use
* Go the Extra Mile
So get ready to improve your school performance-and study hard for success!

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How to calculate isoelectric point of protein

Theoretical basis of isoelectric point calculation,

Isoelectric point (pI) is a pH in which net charge of protein is zero. In case of proteins isoelectric point mostly depends on seven charged amino acids: glutamate (δ-carboxyl group), aspartate (ß-carboxyl group), cysteine (thiol group), tyrosine (phenol group), histidine (imidazole side chains), lysine (ε-ammonium group) and arginine (guanidinium group). Additonally, one should take into account charge of protein terminal groups (NH₂ i COOH). Each of them has its unique acid dissociation constant referred to as pK.

Moreover, net charge of the protein is in tight relation with the solution (buffer) pH. Keeping in main this we can use Henderson-Hasselbach equation to calculate protein charge in certain pH:

- for negative charged macromolecules:

where pK_n is the acid dissociation constant of negatively charged amino acid

- for positive charged macromolecules:

 

where pK_p is the acid dissociation constant of positively charged amino acid

As you can see, only pH of buffer is variable in equations. If we successively change this value, finally we will find isoelectric point of analyzed protein. The knowledge of isoelectric point is of great significance in biochemistry (mainly in elecrophoresis and isofocusing techniques), because it allows to match proper environment before the experiment starts.

Generally, macromolecules are positively charged and on the other hand, above proteins isoelectric point, their charge is negative.For example, during electrophoresis, direction of proteins migration, depends only from their charge. If buffer pH (and as a result gel pH) is higher than protein isoelectric point, the particles will migrate to the anode (negative electrode) and  if the buffer pH is lower than isoelectric point they will go to the cathode. In situation when the gel pH and the protein isoelectric point are equal, proteins do not move at all.
Using above formulae, we can calculate theoretical isoelectric point. The result will be almost surely different than real isoelectric point. It is mainly because many proteins are chemically modified (amino acids can be phosphorylated, methylated, acetyleted etc.), which change their charge. Problematic is also the occurrence of cysteines (negative charge) which can oxidise and form disulfide bond in protein. Therefore, they will become cystines, which do not express any charge.
Nevertheless, one can approximately calculate protein isoelectric point which is ± 0.5 of exact isoelectric point. The most critical moment during isoelectric point determination is usage of appropriate pK values. Unfortunately, there is no agreement in this matter. Each source gives different pKs. some are given below:

Isoelectric Point

The isoelectric point (pI), sometimes abbreviated to IEP, is the pH at which a particular molecule or surface carries no net electrical charge.

Amphoteric molecules called zwitterions contain both positive and negative charges depending on the functional groups present in the molecule. The net charge on the molecule is affected by pH of their surrounding environment and can become more positively or negatively charged due to the loss or gain of protons (H⁺). The pI is the pH value at which the molecule carries no electrical charge or the negative and positive charges are equal.

Surfaces naturally charge to form a double layer. In the common case when the surface charge-determining ions are H⁺/OH^-, the net surface charge is affected by the pH of the liquid in which the solid is submerged. Again, the pI is the pH value of the solution at which the surfaces carries no net charge.

The pI value can affect the solubility of a molecule at a given pH. Such molecules have minimum solubility in water or salt solutions at the pH which corresponds to their pI and often precipitate out of solution. Biological amphoteric molecules such as proteins contain both acidic and basic functional groups. Amino acids which make up proteins may be positive, negative, neutral or polar in nature, and together give a protein its overall charge. At a pH below their pI, proteins carry a net positive charge; above their pI they carry a net negative charge. Proteins can thus be separated according to their isoelectric point (overall charge) on a polyacrylamide gel using a technique called isoelectric focusing, which uses a pH gradient to separate proteins. Isoelectric focusing is also the first step in 2-D gel polyacrylamide gel electrophoresis.

(source: wikipedia)

What is the Origin of Viruses?

Origin of Viruses
Three theories have been put forward to explain the origin of viruses. These theories are highly speculative and are as follows :

Survivors of Pre-Cellular First Living Inhabitants of the Earth
This theory intimately rests on the theory of origin of life on Earth. Life, according to this theory, originated from simple inorganic compounds by a slow biochemical evolution of “ordinary” chemical reactions spread over millions and millions of years.

It is speculated that during the course of origin of life on Earth somewhere at the stage when complex chemical molecules united to form still more complex molecules which could mate with still other metastable molecules till a relatively large molecule (like nucleoprotein) capable of growth and division, a simple virus or a protovirus may have originated (Haldane, 1954; Fraser, 1967). This theory, however, enjoys some insurmountable objections.

Present day viruses are all obligate parasites and it is difficult to conceive of their origin before the origin of their hosts (cells) which are at a far higher scale of evolution. Viruses use the same genetic code as cellular organisms and depend solely and entirely on ribosomes, transfer RNAs and enzymes of the host cell for protein biosynthesis. Moreover, viral nucleic acid has the same properties and the same mode of replication as the nucleic acid of cellular organisms.

Regression from More Highly Evolved Free-Living Microorganisms/Cells
Viruses are considered to have originated by retrogressive evolution from free-living cells, according to this theory. A parasite evolves retrogressively as it takes the ready made metabolites from its host instead of synthesizing them himself.

If the parasite continues to evolve retrogressively then, to save labour and energy, it would slowly loss some of its physiological, morphological and even genetical functions that become super-numerary in its new ecological niche and new mode of biological existence. A parasite would, therefore, get regressed to a much simpler organism. Obligate intracellular parasitism is the most specialized type of parasitism and such a parasite would ultimately possess only the bare minimum and this minimum is the possession of a nuclei acid (to ensure genetic continuity) enclosed within a protein shell (to ensure safety of the nucleic acid).

Shedding of all unnecessary morphological, physiological and genetical materials would necessarily reduce the size. A formerly free-living organism would thus be transformed into a virus. Green (1935), Laidlow (1938) and Burnet (1945) support the theory of retrogressive origin of viruses but the same is opposed by Luria and Darnell (1967) and Fenner (1968).

Derived from Normal Constituents of the Cell
An eukaryotic cell possesses organelles like chloroplasts and mitochondria which self-replicating semi-autonomous structures and reproduce their like. Chloroplasts and mitochondria increase in size and then divide while kinetosome is synthesized near a pre-existing one by assembly from the tubular materials. Besides they possess DNA which is functional and possesses its own mutational history, codes for the synthesis of mRNA and also presumably for protein.

Mitochondria mutate to non­functional forms in Neurospora and yeasts, while chloroplasts mutate to undeveloped, colourless proplastids in algae and higher plants. These mutations are based on genetic changes. Cells also contain certain organelles that exceptionally undergo autonomous unrestricted replications; examples are the centrioles in Marsilea and sperms and nuclear genes in the amphibian oocytes.

Viruses resemble above mentioned cellular organelles in chemical composition, possession of nucleic acid, genetic continuity of genome, independent mutational history, capacity to replicate independently under their own genetic control and also under the overall regulatory control of and within the premises of the host cell.

Many of the cellular organelles or factors possess some of the distinctive characters of viruses, or more specifically, of viral genetic determinant (reproductive independence, evolutionary independence, independent cell to cell transfer and infectivity and pathogenicity) while others could be conferred on them by a specific arrangement of nucleotides. Viruses could, therefore, be derived from any or several of these cellular components and it is possible that different viruses have originated differently. Some of the possibilities are given below:

1. Primordial self-replicating molecules may have mutated to regain the capacity to enter ('infect') the cell and then integrate with it. Such a molecule would be a 'virus'.

2. Some plasmids or even chromosomal segments may have evolved by merging of some primitive self-replicating molecules with the cellular genome. If this s true then it conceivable that some of the genes or groups of genes may revert to their ancestral habit and may have regained/evolved the genetic independence and independence and independent transfer of this genetic material. This would result in the ‘virus’.

3. Some genes of the cell could have escaped of the control mechanisms of the cell and may have acquired the capacity of autonomous replication independent of the division of the cell and capacity of independent transfer. Integration of these genes with the host genome would give us a prophage. Origin of bacteriophage from such prophage DNA has been outlined by Lindegren (1962). Luria and Darnell (1967) also suggest that bacteriophages containing DNA may have evolved from a number of genetic transfer elements (like F factor, bacteriocinogenic factor, etc.) occurring in the prokaryotic cells.

4. DNA viruses of eukaryotic cells may have originated from the functional DNA of cellular organelles (e.g., mitochondria and chloroplast) rather than for nuclear DNA (Matthews, 1970).

5. Origin of DNA plant viruses is somewhat more difficult to understand since there is no definite information with respect to the integration of plant viral nucleic acid into the genome of the plant cell. There is, however, some suggestive evidence in this connection. Some experimental evidence suggests that cut surfaces of barley seeds take up the DNA of the bacterium Micrococcus lysodeikticus and that it integrates into nuclear DNA of barley and replicates (Ledous and Huort, 1968).

In short, therefore, viruses may have originated from cell constituents which escape the control mechanisms of the cell, regained/developed the capacity of autonomous self-replication and ability to mediate their own independent cell to cell transfer and could enter or infect cells to which they did not belong.

Practise session for Biology students

Consider the 19 enzymes in the direct pathway for the conversion of all carbon atoms in glucose to carbon dioxide. (This pathway includes the glycolytic path to pyruvate, pyruvate dehydrogenase complex, and the entire TCA cycle.) Do not include auxiliary reactions, such as the respiratory chain, oxidative phosphorylation, or the glycerol phosphate shuttle..

Write the complete name for all enzymes in the above pathway that catalyse the following:

1. an oxidation-reduction reaction.

2. the intramolecular migration of a functional group.

3. the removal of water from a single substrate molecule.

4. the addition of water to a single substrate molecule.

5. a reaction in which there are more bonds with high group-transfer potential in the products than in the substrates.

6. a reaction in which there fewer bonds with high group-transfer potential in the products than in the substrates.

7. a reaction in which a saturated C-C bond is oxidized to an unsaturated C=C bond.

8. a reaction in which a vitamin or a derivative of a vitamin is involved as substrate and/or product.