Physical Principles and Techniques of Protein Chemistry, Part 2Sydney J. Leach, Sidney J. Leach Physical Principles and Techniques of Protein Chemistry, Part B deals with the theories and application of selected physical methods in protein chemistry evaluation. This book is divided into seven chapters that cover the ultracentrifugal analysis, light scattering, infrared (IR) methods, nuclear magnetic resonance (NMR) spectroscopy, and differential thermal analysis of protein properties. This text first describes the fundamental ideas and methodology of sedimentation analysis of ideal noninteracting solutes and the problems of nonideality and solute-solute interaction. This book then deals ... |
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Page 368
... residues , the basic form of imidazole groups of histidine residues , or the amide groups of the backbone and asparagine and glutamine residues . They may bear formal charges , such as the nega- tive carboxylate groups of aspartic and ...
... residues , the basic form of imidazole groups of histidine residues , or the amide groups of the backbone and asparagine and glutamine residues . They may bear formal charges , such as the nega- tive carboxylate groups of aspartic and ...
Page 379
... residues given in Table I. For example , residues 12 , 48 , 81 , 113 , and 116 are quite clearly exposed to solvent , and 64 and 119 appear to be adequately exposed at one imid- azole nitrogen atom . Residues 24 , 82 , and 93 are ...
... residues given in Table I. For example , residues 12 , 48 , 81 , 113 , and 116 are quite clearly exposed to solvent , and 64 and 119 appear to be adequately exposed at one imid- azole nitrogen atom . Residues 24 , 82 , and 93 are ...
Page 380
... residues . B. VARIABILITY WITHIN A CLASS OF EXPOSED BINDING SITES Considering the variability of the environments of the exposed histidyl residues in myoglobin , it is to be expected that differences in reactivity will be found . For ...
... residues . B. VARIABILITY WITHIN A CLASS OF EXPOSED BINDING SITES Considering the variability of the environments of the exposed histidyl residues in myoglobin , it is to be expected that differences in reactivity will be found . For ...
Contents
Ultracentrifugal Analysis J H Coates | 1 |
Glossary of Symbols | 2 |
Introduction | 3 |
Copyright | |
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absorption acid amino anions atoms axial ratio band beam binding Biol bond Bradbury calculated capillary cell centrifugal chain changes Chem chemical shifts complex component concentration constant copper(II denaturation density gradient dependence determined dilution Doty effect electron ellipsoid enzyme equation extrapolation field Fraser frequency fringe Gurd histidine hydrogen ion imidazole imidazole groups instrument interaction intrinsic viscosity Jardetzky length light scattering light-scattering line width lysozyme macromolecule magnetic measured meniscus metal ion method molecular weight molecule myoglobin nuclei observed obtained optical density optical system partial specific volume particle PBLG peak peptide Phys plot Polymer Sci Proc protein solution protons random coil Rayleigh reference refractive index relaxation residues resonance RNase rotation rotor sample schlieren Section sedimentation coefficient sedimentation equilibrium shearing stress slit solvent spectra spectrum speed structure studies Tanford technique temperature Timasheff tion transition ultracentrifuge values velocity Vinograd viscometer zero zone