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 ... |
From inside the book
Results 1-3 of 72
Page 283
... resonance frequency for a particular proton is a sensi- tive indicator of its chemical environment . B. THE CHEMICAL SHIFT σ eff So far it has been assumed that the resonance frequency of a nucleus depends only on the applied field and ...
... resonance frequency for a particular proton is a sensi- tive indicator of its chemical environment . B. THE CHEMICAL SHIFT σ eff So far it has been assumed that the resonance frequency of a nucleus depends only on the applied field and ...
Page 295
... resonance signals also sets a limit on the inherent sensitivity of nuclear magnetic resonance . The magnitude of the absorp- tion signal observed depends on the amount of energy absorbed from H1 , which must remain small compared with ...
... resonance signals also sets a limit on the inherent sensitivity of nuclear magnetic resonance . The magnitude of the absorp- tion signal observed depends on the amount of energy absorbed from H1 , which must remain small compared with ...
Page 302
... resonance is extremely sharp and lies at very high fields . On the & scale ( Eq . 4 ) , the reference has a chemical shift of zero , so that when TMS is the refer- ence most proton resonances have negative & values . Another scale which ...
... resonance is extremely sharp and lies at very high fields . On the & scale ( Eq . 4 ) , the reference has a chemical shift of zero , so that when TMS is the refer- ence most proton resonances have negative & values . Another scale which ...
Contents
Ultracentrifugal Analysis | 10 |
Light Scattering | 12 |
Osmotic Pressure | 13 |
Copyright | |
31 other sections not shown
Other editions - View all
Common terms and phrases
absorption acid angle axial ratio axis band beam binding Biol Bradbury Brice calculated capillary centrifugal chain Chem chemical shifts column complex component concentration dependence constant copper(II denaturation density gradient determined diffusion dilution Doty effect ellipsoid equation experiments extrapolation filters Fraser frequency fringe groups Gurd Holtzer hydrogen increment instrument interaction intrinsic viscosity Kirkwood length light scattering light-scattering linear macromolecule maximum measured meniscus method molecular weight molecule Natl observed obtained optical density optical system parameters partial specific volume particle peak photographic Phys plate plateau plot Polymer Sci Proc procedure protein solution protons radius random coil Rayleigh reference refractive index refractive index increment residues resonance rotation rotor sample Schachman schlieren Section sedimentation coefficient sedimentation equilibrium shearing stress shown in Fig slit solvent spectra spectrum speed structure synthetic boundary Tanford technique temperature Timasheff tion transmittance tube ultracentrifuge values Vinograd viscometer zero Zimm zone