000			04094nam a22002417a 4500
999			_c56071 _d56071
005			20200131142655.0
008			191218b ||||| |||| 00| 0 eng d
020			_a9780387903347
028			_aAtlantic Publishers & Distributors (P) Ltd. _b;7/22,Ansari Road ,Darya Ganj,New Delhi-110002 _c;1105820 _d;12/12/2019
082			_a547.75 SCH
100			_aG E Schulz _a; R Heiner Schirmer
245			_aPrinciples of protein structure _c/G E Schulz
260			_aNew York _b: Springer-Verlag _c, ©1979.
300			_ax, 314 pages _c ; 24 cm
365			_b6599
490			_aSpringer advanced texts in chemistry.
505			_a 1 Amino Acids.- 1.1 The 20 Standard Amino Acids.- 1.2 Why Were Just These Amino Acids Selected?.- 1.3 Colinear Relation Between Nucleic Acids and Polypeptides.- 1.4 Side Chain Properties.- 1.5 Empirical Similarities Between Amino Acid Residues.- Summary.- 2 Structural Implications of the Peptide Bond.- 2.1 Synthesis on Ribosomes.- 2.2 Peptide Bond Dimensions.- 2.3 Steric Hindrance.- 2.4 Conformational Energy.- 2.5 cis versus trans Configuration.- Summary.- 3 Noncovalent Forces Determining Protein Structure.- 3.1 Dispersion Forces and Electron Shell Repulsion.- 3.2 Electrostatic Interactions.- 3.3 Van der Waals Potentials.- 3.4 Hydrogen Bonds.- 3.5 Entropic Forces.- 3.6 Molecular Packing.- Summary.- 4 The Covalent Structure of Proteins.- 4.1 Chain Assemblies.- 4.2 Disulfide Bonds.- 4.3 Enzyme-Controlled Modifications of the Main Chain.- 4.4 Enzyme-Controlled Side Chain Modifications.- Summary.- 5 Patterns of Folding and Association of Polypeptide Chains.- 5.1 Secondary Structure.- 5.2 Supersecondary Structures.- 5.3 Structural Domains.- 5.4 Globular Proteins.- 5.5 Aggregates of Globular Proteins.- 5.6 Hierarchy of Levels.- Summary.- 6 Prediction of Secondary Structure from the Amino Acid Sequence.- 6.1 Probabilistic Methods.- 6.2 Physico-Chemical Methods.- 6.3 Application of Prediction Methods.- 6.4 Evaluation of Prediction Methods.- 6.5 Emerging General Results.- Summary.- 7 Models, Display, and Documentation of Protein Structures.- 7.1 Structural Ingredients.- 7.2 Representations of Complete Structures.- 7.3 Abstract Chain Fold Representations.- Summary.- 8 Thermodynamics and Kinetics of Polypeptide Chain Folding.- 8.1 Thermodynamic Aspects.- 8.2 Speed, Precision, and Limitations of Folding in vitro.- 8.3 Structural Elements in Unfolded Chains.- 8.4 Folding Pathway.- 8.5 The Influence of Ligands.- 8.6 Simulations of the Folding Process.- Summary.- 9 Protein Evolution.- 9.1 Protein Speciation.- 9.2 Phylogeny on the Basis of Protein Structures.- 9.3 Protein Differentiation.- 9.4 Gene Fusion.- 9.5 Convergent Evolution in Proteins.- 9.6 Recognition of Distant Relationships.- Summary.- 10 Protein-Ligand Interactions.- 10.1 Ligand-Binding Sites of Immunoglobulins.- 10.2 Substrate-Binding Sites of Serine Proteases.- 10.3 Haem-Binding Sites.- 10.4 Nucleotide-Binding Sites.- 10.5 Binding Sites for Phosphoryl Groups.- 10.6 Interactions of Proteins With Other Macromolecules.- Summary.- 11 The Structural Basis of Protein Mechanism, Action, and Function.- 11.1 Definitions.- 11.2 Enzyme Catalysis.- 11.3 Biological and Medical Aspects of Protein Action and Function.- 11.4 Skeletal Muscle, a System in Which Protein Action Can be Related to the Overall Performance of an Organ.- Summary.- Appendix Statistical Mechanics of the Helix-Coil Transition.- A.1 Partition Function.- A.2 Probability of a Residue Being in a Certain Conformation.- A.3 Ising Model.- A.4 Zimm-Bragg Model for Helix-Coil Transition.- A.5 Comparision With Experimental Data.- References.
520			_aNew textbooks at all levels of chemistry appear with great regularity. Our goal, in this series, is to pinpoint areas of chemistry where recent progress has outpaced what is covered in any available textbooks, and then seek out and persuade experts in these fields to produce relatively concise but instructive introductions to their fields.
650			_aProteins
655			_aMacromolecular Substances.
700			_aR Heiner Schirmer
942			_cBOOK