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 366
... binding ( Klotz , 1952 , 1954 ) and anion binding ( Scatchard , 1949 ) followed , and was correlated closely with hydrogen ion binding ( Scatchard et al . , 1954 ; Gurd and Wil- cox , 1956 ; Edsall and Wyman , 1958 ) . Interactions of ...
... binding ( Klotz , 1952 , 1954 ) and anion binding ( Scatchard , 1949 ) followed , and was correlated closely with hydrogen ion binding ( Scatchard et al . , 1954 ; Gurd and Wil- cox , 1956 ; Edsall and Wyman , 1958 ) . Interactions of ...
Page 396
... BINDING SITES The identification of the binding site of an ion involves the recognition of which groups in the protein are responsible for binding the ion . It is rare for studies in solution to yield a complete description of the ...
... BINDING SITES The identification of the binding site of an ion involves the recognition of which groups in the protein are responsible for binding the ion . It is rare for studies in solution to yield a complete description of the ...
Page 413
... binding site and reflected its protein environment . Titration in the range of pH where appreciable displace- ment of protons from peptide bonds occurs could be interpreted approxi- mately in terms of binding of the copper ( II ) , and ...
... binding site and reflected its protein environment . Titration in the range of pH where appreciable displace- ment of protons from peptide bonds occurs could be interpreted approxi- mately in terms of binding of the copper ( II ) , and ...
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