Optical Rotatory Dispersion. Its Application to Protein Conformation.

作者: E. F. Woods , I. J. O’;Donnell

DOI: 10.1007/978-3-642-45993-1_11

关键词:

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.

参考文章(41)
E. M. BRADBURY, A. R. DOWNIE, A. ELLIOTT, W. E. HANBY, Screw Sense of the α-Helix in Poly-β-benzyl- L -aspartate Nature. ,vol. 187, pp. 321- 321 ,(1960) , 10.1038/187321A0
W. Kauzmann, Some factors in the interpretation of protein denaturation. Advances in Protein Chemistry. ,vol. 14, pp. 1- 63 ,(1959) , 10.1016/S0065-3233(08)60608-7
W. Klyne, Optical rotatory dispersion Tetrahedron. ,vol. 13, pp. 29- 47 ,(1961) , 10.1016/S0040-4020(01)92203-3
K. Linderstrøm-Lang, John A. Schellman, The structure of insulin as compared to that of Sanger's A-chain. Biochimica et Biophysica Acta. ,vol. 15, pp. 156- 157 ,(1954) , 10.1016/0006-3002(54)90116-X
CAROLYN COHEN, Optical rotation and polypeptide chain configuration in proteins. Nature. ,vol. 175, pp. 129- 130 ,(1955) , 10.1038/175129A0
P. Doty, R. D. Lundberg, THE CONTRIBUTION OF THE α-HELICAL CONFIGURATION TO THE OPTICAL ROTATION OF POLYPEPTIDES AND PROTEINS Proceedings of the National Academy of Sciences of the United States of America. ,vol. 43, pp. 213- 222 ,(1957) , 10.1073/PNAS.43.2.213
Kazutomo Imahori, Rotatory behavior of protein denaturation. Biochimica et Biophysica Acta. ,vol. 37, pp. 336- 341 ,(1960) , 10.1016/0006-3002(60)90242-0
John A. Schellman, The Factors Affecting the Stability of Hydrogen-bonded Polypeptide Structures in Solution The Journal of Physical Chemistry. ,vol. 62, pp. 1485- 1494 ,(1958) , 10.1021/J150570A005
J. C. KENDREW, R. E. DICKERSON, B. E. STRANDBERG, R. G. HART, D. R. DAVIES, D. C. PHILLIPS, V. C. SHORE, Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution Nature. ,vol. 185, pp. 422- 427 ,(1960) , 10.1038/185422A0