Physical Principles and Techniques of Protein Chemistry Part C, Part 3Sydney Leach Physical Principles and Techniques of Protein Chemistry, Part C focuses on the effects of intermolecular interactions that are transmitted between ligands and proteins and from protein to protein. This book discusses the density and volume change measurements; direct volume change; osmotic pressure; and small-angle X-ray scattering. The theory of particulate scattering; pulsed nuclear magnetic resonance; absorption of water by diamagnetic molecules; and use of least squares in data analysis are also elaborated. This text likewise covers the iteration process; optical rotatory dispersion and the main chain conformation of proteins; and basic relations for optically active molecules. Other topics include the circular dichroism, secondary structure of proteins, visible rotatory dispersion, and peptide cotton effects. This publication is intended for protein chemists, but is also useful to biologists, medical practitioners, and students researching on protein chemistry. |
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Page xi
... structure toward one incorporating Linderstr¢m—Lang's concept of motility. This shift in thinking owes much to the ... B of the treatise, the stress varying between the theory, the experimental execution, and the problems of interpreting ...
... structure toward one incorporating Linderstr¢m—Lang's concept of motility. This shift in thinking owes much to the ... B of the treatise, the stress varying between the theory, the experimental execution, and the problems of interpreting ...
Page 26
... structure, which is not very intricate in histone, contributes to the suppression of a normal volume change. By ... structure, and (b) the minor contributions arising from conformational arrangements Of the polypeptide and the variety of ...
... structure, which is not very intricate in histone, contributes to the suppression of a normal volume change. By ... structure, and (b) the minor contributions arising from conformational arrangements Of the polypeptide and the variety of ...
Page 47
... (b) the nature of the solvent medium, and to a lesser extent (c) differences in temperature Of the various ... structure of proteins by causing hydrolysis, covalent additions, or complete unfolding are of course, excluded, in these ...
... (b) the nature of the solvent medium, and to a lesser extent (c) differences in temperature Of the various ... structure of proteins by causing hydrolysis, covalent additions, or complete unfolding are of course, excluded, in these ...
Page 117
... structure of proteins may be studied with a minimum of the complexity, ambiguity, and data-handling problems ... B may be utilized for the estimation of ion binding to proteins at relatively high ionic strengths. For this purpose, the ...
... structure of proteins may be studied with a minimum of the complexity, ambiguity, and data-handling problems ... B may be utilized for the estimation of ion binding to proteins at relatively high ionic strengths. For this purpose, the ...
Page 155
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Contents
1 | |
77 | |
Chapter 19 SmallAngle Xray Scattering | 141 |
Chapter 20 Pulsed Nuclear Magnetic Resonance | 245 |
Chapter 21 The Use of Least Squares in Data Analysis | 301 |
Chapter 22 Optical Rotatory Dispersion and the Main Chain Conformation of Proteins | 357 |
Chapter 23 Circular Dichroism | 445 |
Author Index | 595 |
Subject Index | 609 |
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Common terms and phrases
a-helix absorption acid Amer angle B-structure Beychok Biochem Biochemistry Biol Blout calculated CD band CD spectra Chem chromophore circular dichroism coefficient Cohn coil concentration conformation constant contribution Cotton effects creatine kinase cross-section defined definition denatured determined dialyzate diffusible components dipole disulfide electron density ellipticity enzyme equation equilibrium exciton experimental Fasman field find first fit function grams helix hemoglobin intensity interaction Kratky lysozyme magnetic measurements membrane method molal mole molecular weight molecule myoglobin negative negative band obtained optical activity ORD curve osmotic pressure parameters partial specific volume peptide Phys Pilz polymer polypeptides positive protein protein solution Pysh radius of gyration random coil residues ribonuclease rotational strength rotatory sample scattering curve Schellman Section shape significant small-angle solvent solvent medium spectrum studies subunits sufficiently temperature theoretical theory Tinoco tion transition tyrosine wavelength Woody X-ray zero