Physical Principles and Techniques of Protein Chemistry, Part 1Sydney J. Leach Physical Principles and Techniques of Protein Chemistry, Part A deals with the principles and application of selected physical methods in protein chemistry evaluation. This book is organized into nine chapters that cover microscopic, crystallographic, and electrophoretic techniques for protein conformational perturbations evaluation. This text first presents a general account of electron microscopy, its specimen preparation, optimum conditions for high resolution, measurement of electron micrographs, and illustrative examples of protein study. This book then examines the different types of map ... |
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Page 220
... salt - free solution compared with that in 1 M NaCl ( Weber and Rosenheck , 1964 ) . The influence of environmental factors is evident also in copolymers of tyrosine where it is incorporated as a " block . " In this form the quantum ...
... salt - free solution compared with that in 1 M NaCl ( Weber and Rosenheck , 1964 ) . The influence of environmental factors is evident also in copolymers of tyrosine where it is incorporated as a " block . " In this form the quantum ...
Page 362
... salt - free condition . The polymerization was shown to consist of head - to - head , head - to - tail , and antiparallel side - by - side associations . Kobayashi , Asai , and Oosawa ( 1964 ) followed the polymerization of actin by the ...
... salt - free condition . The polymerization was shown to consist of head - to - head , head - to - tail , and antiparallel side - by - side associations . Kobayashi , Asai , and Oosawa ( 1964 ) followed the polymerization of actin by the ...
Page 409
... salt concentration and pH by addition of a small quantity of a buffer of appropriate composition ( Cann , 1959 ) but this procedure is awkward . momentarily , stabilized by an opposing gradient of salt concentration 8. ELECTROPHORESIS 409.
... salt concentration and pH by addition of a small quantity of a buffer of appropriate composition ( Cann , 1959 ) but this procedure is awkward . momentarily , stabilized by an opposing gradient of salt concentration 8. ELECTROPHORESIS 409.
Contents
Electron Microscopy of Globular Proteins | 2 |
Ultraviolet Absorption | 3 |
The Enhancement of Contrast | 21 |
Copyright | |
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absorption absorption spectrum applied atoms axis Biochem Biol Biophys birefringence boundary bovine serum albumin buffer calculated Cann Chem chromophores coefficient components concentration curve denaturation density determined dielectric constant dielectric increment dielectric relaxation difference spectrum diffraction dipole moment Edelhoch effects electric birefringence electric field electron microscope electrophoresis elution volume emission enzyme equation equilibrium excitation experimental factor film fluorescence fraction frequency gel filtration gradient groups intensity interactions ionic strength ions lens light linear macromolecules measured method micrographs migration mobility molar molecular weight molecules moving-boundary observed obtained optical ovalbumin parameter particles peaks permanent dipole perturbation phase phenolic photomultiplier Phys plot polarization polymer produced protein quantum yield ratio reaction relaxation residues resolution resolving power ribonuclease scattering shadow shown in Fig solution solvent specimen spectra structure studies technique temperature theoretical theory tion tryptophan tyrosine unit cell values wavelength Weber Winzor zone