作者: E. F. Woods , I. J. O’;Donnell
DOI: 10.1007/978-3-642-45993-1_11
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摘要: Optical rotation has been found to be one of the most convenient methods following denaturation proteins. Generally speaking can defined as a process or sequence processes in which spatial arrangement polypeptide chains within molecule is changed from that typical native protein more disordered (Kauzmann 1959). The terms “configuration”, “conformation” and “state folding” are widely used for arrangement. It probably best follow suggestion Blout (1960) restrict use “configuration” its original sense, i.e. around an asymmetric carbon atom, shape entirety. properties discussed previous Chapter i.e., viscosity, diffusion, sedimentation, light scattering — all furnish information on overall proteins other macromolecules changes this with environment. Thus Doty, Bradbury Holtzer (1956) were able show using these methods, together streaming birefringence, poly-γ-benzyl-L-glutamate could exist two conformations, α-helix solvated randomly coiled form, depending solvent. change random coil was accompanied by marked optical rotatory polypeptides. expected α-helical structure should contribute power since helices not superimposable their mirror images. work polypeptides shown dispersion capable providing folding chain accompanying denaturation.