Introduction to Protein Science has 12 ratings and 1 review. Carolyn said: This is a beautiful and accessible-yet-thorough introduction to proteomics. Apurvai By Pu La Deshpande Free.

Lesk, Arthur M. Divan E Shams E Tabrizi Pdf Printer. , Oxford University Press, Oxford, United Kingdom, 2004, 307 pp., ISBN 0‐19‐926511‐9, $51.95. This book provides a lucid, authoritative, multi‐disciplinary, yet succinct introduction to the science of proteins. It provides a broader and less specialized starting point for two previous books by Lesk, Introduction to Protein Architecture and Introduction to Bioinformatics, thereby completing a trilogy.

Thus, the present work, Introduction to Protein Science, complements rather than competes with more specialized treatments of protein structure, such as Lesk's Introduction to Protein Architecture (Oxford, 2001) or Introduction to Protein Structure by Carl Branden and John Tooze (Garland, 2nd Edition, 1999). Chapter 1 offers a lovely brief introduction to the central dogma, with emphasis on ribosome structure and function, with attention to history—in only 10 pages. The style is engaging. “Cells take ribosomes very seriously.” (Did you know that the 15,000 ribosomes in each Escherichia coli cell constitute 25% of its mass?) About the crystal structure of the ribosome: “The results came as a shock.

The ribosome is a ribozyme.” Chapter 2 strongly emphasizes protein three‐dimensional structure. The title, Genomics and Proteomics, may be somewhat of a misnomer, because only the first few of 55 pages deal with genomics, and the chapter gets to proteomics in the strict sense only at the end. Alternate splicing, post‐translational changes, primary, secondary, tertiary, and quaternary protein structure, topology, domains, and chaperones are explained, followed by a survey of functional and structural categories of proteins, each with examples. Students will be engaged when some of the examples highlight the clinical consequences of mutations, relating them to structural consequences.

A clear and very useful distinction is drawn between “similarity” and “homology,” giving examples. Chapter 2 finishes with introductions to proteomics, mass spectrometry, microarrays, and bioinformatics. Chapter 3 covers chemical structure and activity of proteins in about 50 pages. It includes the basics of protein chemical structure and bonding, spectroscopic methods, and introduces x‐ray crystallography, nuclear magnetic resonance, and cryo electron microscopy. Structure is discussed vis a vis catalysis, conformational changes, and regulation of function, with hemoglobin used as a detailed example. Chapter 4 deals with evolution of protein structure and function, structure and domain classification. Globins, NAD‐binding domains of dehydrogenases, and visual pigments are detailed examples.

Evolution of new function is discussed in terms of divergence, recruitment, domain duplication, and swapping. Protein engineering, folding, prediction, and design make up Chapter 5. There is a rather detailed discussion of folding (14 pages) including thermodynamics, kinetics, equilibrium, molten globule, denaturants, misfolding, and chaperonins. Homology modeling and threading are also here. Protein oligomerization and protein‐DNA interaction are covered in 30‐some pages in Chapter 6, including viruses and membrane proteins. Proteins in disease, Chapter 7, completes the book.

Diseases of protein aggregation, such as Alzheimer's, Huntington's, and prions, are discussed, along with considerable detail on antibodies and major histocompatibility proteins. Eddie Bauer Car Seat 22 740 Hpn Manual High School more. Each chapter begins with a detailed list of learning goals, and finishes with websites, exercises (short answers), problems (longer answers, sometimes with calculations), and “weblems” to provide experience with on‐line tools. Answers are not provided, which may limit the usefulness of some questions, but this is in part because of the open‐ended nature of many questions. Hp Pavilion Dv6700 Xp Install Cd on this page. PDB identification codes are given in the legends of most figures, making computer visualization of the illustrated molecules easily accessible.

In addition to the many strengths listed above, there are also some weaknesses. Lesk conveys the impression that all proteins must fold into a compact, low‐energy, native state in order to function. I found no mention of the concept of intrinsically unstructured or disordered regions of proteins, present in 40% of proteins by one estimate, with roughly 10% of proteins predicted to be fully disordered [, ]. Neither “disordered” nor “unstructured” appear in the index nor glossary. The Protein Data Bank is introduced in Chapter 2, but no estimate is given of the percentage of proteins genome‐wide that have empirically known structure (which is less than a few percent). Although ab initio structure prediction of novel folds from sequence is introduced nicely in Chapter 5, and critical assessment of structure prediction is mentioned, the present success levels are not quantitated, nor is it made clear that for most purposes useful predictions of tertiary structure cannot be achieved from sequence alone.