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 48
... known levels using a precision syringe or microm- eter syringe . This is necessary to ensure that the solution column is always very slightly shorter than the solvent column as shown in Fig . 16 , so that the complete solution column is ...
... known levels using a precision syringe or microm- eter syringe . This is necessary to ensure that the solution column is always very slightly shorter than the solvent column as shown in Fig . 16 , so that the complete solution column is ...
Page 67
... known , as is c , the equations can be solved for c , and c2 and the equilibrium constant K = c2 / ( c1 ) 2 can be calculated . For a system in which each species behaves as if it were ideal , the same equilibrium constant should be ...
... known , as is c , the equations can be solved for c , and c2 and the equilibrium constant K = c2 / ( c1 ) 2 can be calculated . For a system in which each species behaves as if it were ideal , the same equilibrium constant should be ...
Page 200
... known molality is prepared by mixing known weights of the two com- ponents . This is used as reference and dilution solvent . A concentrated stock solution of protein ( 50-80 gm / liter ) is prepared in the aqueous medium . Increments ...
... known molality is prepared by mixing known weights of the two com- ponents . This is used as reference and dilution solvent . A concentrated stock solution of protein ( 50-80 gm / liter ) is prepared in the aqueous medium . Increments ...
Contents
Ultracentrifugal Analysis | 10 |
Light Scattering | 12 |
Osmotic Pressure | 13 |
Copyright | |
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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