Biophysical Chemistry: Part I: The Conformation of Biological MacromoleculesThree-part series remains the definitive text on the physical properties of biological macromolecules and the physical techniques used to study them. It is appropriate for a broad spectrum of advanced undergraduate and graduate courses and serves as a comprehensive reference for researchers. Part I: The Conformation of Biological Macromolecules 1980, paper, 365 pages, 158 illustrations 0-7167-1188-5 Part II: Techniques for the Study of Biological Structure and Function 1980, paper, 365 pages, 158 illustrations 0-7167-1190-7 Part III: The Behavior of Biological Macromolecules 1980, paper, 597 pages, 243 illustrations 0-7167-1192-3 |
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Contents
PARTI | 1 |
Other Hydrodynamic Techniques | 12 |
Kinetics of Ligand Interactions | 16 |
Statistical Mechanics and Kinetics of Nucleic Acid Interactions | 23 |
Box 11 A general scheme for multicomponent analysis | 37 |
Relationship between structural and functional similarity | 122 |
Box 25 Symmetry operations | 132 |
The quaternary structure of aspartate transcarbamoylase | 139 |
Structure of Nucleic Acids | 155 |
Other Biological Polymers | 207 |
Conformational Analysis and Forces That Determine | 253 |
Box 52 Derivation of expression for partial molar entropy | 284 |
Conformational Analysis and Forces That Determine | 308 |
Box 63 Surface tension effect | 337 |
Appendix A Review of Elementary Matrix Algebra | 343 |
Appendix B Answers to Problems | 343 |
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Common terms and phrases
active allowed amino acid angles appear arrangement association atoms axis backbone bacteriophage base pairs binding biological bonds calculations cell Chapter charges chemical complex components composition concentration conformation consider consistent constant contacts contain detailed determined discussed distance disulfide double effects energy example exist folding formation four fraction function given glycophorin groups helices helix hemoglobin hydrogen bonds identical illustrated important indicate individual interactions involved known length lipid measurements membrane mole molecular molecules native normal Note nucleic acids observed occur ordered organized particular peptide physical polypeptide position possible predicted properties protein quaternary structure regions residues rotation secondary structure separation sequence sheets shown in Figure side chains similar simple single solution solvent specific stabilizing strands studies subunits sugar surface symmetry Table techniques tertiary structure tRNA types units values various weight