SIMPLE TECHNIQUES FOR THE QUANTIFICATION OF PROTEIN SECONDARY STRUCTURE BY H-1-NMR SPECTROSCOPY

被引:91
作者
WISHART, DS [1 ]
SYKES, BD [1 ]
RICHARDS, FM [1 ]
机构
[1] UNIV ALBERTA,DEPT BIOCHEM,MRC,PROT STRUCT & FUNCT GRP,EDMONTON T6G 2H7,ALBERTA,CANADA
关键词
NMR; CHEMICAL SHIFT; SECONDARY STRUCTURE; PROTEIN STRUCTURE; CIRCULAR DICHROISM;
D O I
10.1016/0014-5793(91)81155-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Previous work by Wishart et al. (in press) and others [(1989) J. Magn. Reson. 83, 441-449; (1990) J. Magn. Reson. 90, 165-176] has shown a strong tendency for protein secondary structure to be manifested in H-1 NMR chemical shifts. Based on these earlier results, two techniques have been developed for the quantification of secondary structure in proteins. Both methods allow for the rapid and accurate determination of the percent content of helix, coil, and beta-strand based on the integration (or peak enumeration) of selected portions of either 1-D or 2-D H-1 NMR spectra These new and very simple procedures have been found to compare quite favorably to other well established techniques for secondary structure determination such as CD, Raman and IR spectroscopy.
引用
收藏
页码:72 / 80
页数:9
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