PEPTIDE PROTEIN-STRUCTURE ANALYSIS USING THE CHEMICAL-SHIFT INDEX METHOD - UPFIELD ALPHA-CH VALUES REVEAL DYNAMIC HELICES AND ALPHA-L SITES

被引:26
作者
ANDERSEN, NH
CAO, BL
CHEN, CP
机构
[1] Department of Chemistry, University of Washington, Seattle
关键词
D O I
10.1016/0006-291X(92)90691-D
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
The α-CH shifts observed by 1H NMR for medium-sized peptides and for an unusual small protein, hevein, which has a high density of αL conformations within its 43 residue length, reveal that the recently introduced chemical shift index (CSI) analysis places short dynamic helices (αR) and αL residues in the same category as stable helices. The method appears to be a promising addition to the arsenal of methods for peptide structure analysis and is clearly not limited to rigid protein systems. © 1992.
引用
收藏
页码:1008 / 1014
页数:7
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