OPTICAL MEASUREMENT OF A SOLVENT-INDUCED ISOMERIZATION IN A PROLINE-CONTAINING HEXAPEPTIDE

被引：9

作者：

GAREL, JR ^{[1
]}

SIFFERT, O ^{[1
]}

机构：

[1] INST PASTEUR, DEPT BIOCHIM & GENET MICROBIENNE, UNITE CHIM PROTEINES, F-75724 PARIS, FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 89卷 / 02期

关键词：

D O I：

10.1016/0006-291X(79)90671-5

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 hexapeptide Gly-Gly-Pro-Tyr-Gly-Gly was synthesized and its tyrosine residue converted to nitrotyrosine by reaction with tetranitromethane. When diluted from dimethylsulfoxide into aqueous solution, the nitrated hexapeptide undergoes a slow conformational change characterized by a change in the ionization state of the nitrotyrosine group. This slow reaction is not observed with peptides containing nitrotyrosine and no proline. The rate and activation enthalpy of the slow conformational change suggest that it could be due to proline cis-trans isomerization. The possibility of measuring the rate of cis-trans isomerization of proline residues in a polypeptide chain is discussed.

引用

页码：591 / 597

页数：7

共 13 条

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