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 302
... chemical shift of zero , so that when TMS is the refer- ence most proton ... shifts measured with DSS agree well with those based on TMS in solvents in ... chemical shifts do not normally depend on the temperature , and the majority of ...
... chemical shift of zero , so that when TMS is the refer- ence most proton ... shifts measured with DSS agree well with those based on TMS in solvents in ... chemical shifts do not normally depend on the temperature , and the majority of ...
Page 333
... chemical shift ( 8 ) to the total NAG concentration ( So ) in the presence of constant concentrations of lysozyme . The linear plots of So vs. 1/8 yielded both the chemical shifts of the bound forms and also the affinities of the methyl ...
... chemical shift ( 8 ) to the total NAG concentration ( So ) in the presence of constant concentrations of lysozyme . The linear plots of So vs. 1/8 yielded both the chemical shifts of the bound forms and also the affinities of the methyl ...
Page 337
... shifts due to peptide bond formation to which we can now add shifts due to secondary and tertiary structure . A recent comparison of amino acid chemical shift data with the RNase spectrum is given by Mandel ( 1965 ) for the 100 MHz ...
... shifts due to peptide bond formation to which we can now add shifts due to secondary and tertiary structure . A recent comparison of amino acid chemical shift data with the RNase spectrum is given by Mandel ( 1965 ) for the 100 MHz ...
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