Structure in Protein Chemistry

The second edition of Structure in Protein Chemistry showcases the latest developments and innovations in the field of protein structure analysis and prediction. The book begins by explaining how proteins are purified and describes methods for elucidating their sequences of amino acids and defining their posttranslational modifications. Comprehensive explanations of crystallography and of noncovalent forces-ionic interactions, hydrogen bonding, and the hydrophobic effect-act as a prelude to an exhaustive description of the atomic details of the structures of proteins. The resulting understanding of protein molecular structure forms the basis for discussions of the evolution of proteins, the symmetry of the oligomeric associations that produce them, and the chemical, mathematical, and physical basis of the techniques used to study their structures. The latter include image reconstruction, nuclear magnetic resonance spectroscopy, proton exchange, optical spectroscopy, electrophoresis, covalent cross-linking, chemical modification, immunochemistry, hydrodynamics, and the scattering of light, X-radiation, and neutrons. These procedures are applied to study the folding of polypeptides and the assembly of oligomers. Biological membranes and their proteins are also discussed. Structure in Protein Chemistry, Second Edition, bridges the gap between introductory biophysical chemistry courses and research literature. It serves as a comprehensive textbook for advanced undergraduates and graduate students in biochemistry, biophysics, and structural and molecular biology. Professionals engaged in chemical, biochemical, and molecular biological research will find it a useful reference.

1. Purification 2. Electronic Structure 3. Sequences of Polymers 4. Crystallographic Molecular Models 5. Noncovalent Forces 6. Atomic Details 7. Evolution 8. Counting Polypeptides 9. Symmetry 10. Chemical Probes of Structure 11. Immunochemical Probes of Structure 12. Physical Measurements of Structure 13. Folding and Assembly 14. Membranes

Jack Kyte, Professor Emeritus in the Chemistry Department at the University of California in San Diego, is well known for his research on the analysis of protein structure. He graduated magna cum laude from Carleton College with a degree in Chemistry. Under the tutelage of Guido Guidotti, he received his graduate degree in the Department of Biochemistry and Molecular Biology at Harvard University in Cambridge Massachusetts. Prof. Kyte joined the Department of Chemistry at the University of California at San Diego in 1974. Prof. Kyte has had a major impact in the prediction and analysis of protein structure. He ran a laboratory investigating the structure and mechanism of sodium and potassium ATPase, an enzyme from plasma membranes responsible for active transport; acetylcholine receptor, a protein in the plasma membrane that transports cations; the receptor for epidermal growth factor, a protein in the plasma membrane that controls cellular growth; and ribonucleotide reductase, a cytoplasmic enzyme responsible for the conversion of ribonucleotides into deoxyribonucleotides. This research was funded by grants from the National Institutes of Health, the National Science Foundation, and the American Heart Association. Prof. Kyte received a Career Development Award from the National Institutes of Health, and served on the editorial board of Biochemistry for six years.