A NMR STUDY OF INTERACTION OF N-TRIFLUOROACETYL-D-PHENYLALANINE WITH ALPHA-CHYMOTRYPSIN

被引：8

作者：

SYKES, BD

机构：

[1] Department of Chemistry Stanford University Stanford

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1968年 / 33卷 / 05期

关键词：

D O I：

10.1016/0006-291X(68)90219-2

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：

The dissociation constant and bound chemical shift for N-trifluoroacetyl-D-phenylalanine exchanging with α-chymotrypsin has been determined by 19F NMR. A computer method is presented for obtaining these constants from chemical shift data. The bound chemical shift appears to be a very sensitive probe for the active site of α-chymotrypsin and reflects changes in the active site with changes in pH. © 1968.

引用

页码：727 / &

共 11 条

[1] SOLVENT EFFECTS IN NUCLEAR MAGNETIC RESONANCE SPECTRA [J].