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 355
... residues are equally involved in the binding sites for each . Subsite C has been implicated in the strong binding of both di- and tri - NAG , and this site involves Trp residues 62 and 63 ; both these residues and Trp - 108 undergo ...
... residues are equally involved in the binding sites for each . Subsite C has been implicated in the strong binding of both di- and tri - NAG , and this site involves Trp residues 62 and 63 ; both these residues and Trp - 108 undergo ...
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 | 1 |
J H Coates Glossary of Symbols 23435 37 | 2 |
Fundamentals of the Method | 5 |
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 region relaxation residues resonance RNase rotation rotor sample schlieren Section sedimentation coefficient shearing stress slit solvent spectra spectrum speed structure studies Tanford technique temperature Timasheff tion transition ultracentrifuge values velocity Vinograd viscometer zero zone