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CHARACTERIZATION OF LOW POPULATED PEPTIDE HELICAL STRUCTURES IN SOLUTION BY MEANS OF NMR PROTON CONFORMATIONAL SHIFTS

被引：34
作者：
BRUIX, M
PERELLO, M
HERRANZ, J
RICO, M
NIETO, JL
机构：
[1] CSIC, INST ESTRUCT MAT, SERRANO 119, E-28006 MADRID, SPAIN
[2] CNRS, CTR BIOPHYS MOLEC, F-45071 ORLEANS 2, FRANCE
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 03期
关键词：
D O I：
10.1016/0006-291X(90)90623-U
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：
A NOE independent NMR method is proposed to characterize unambiguosly residues involved in low populated isolated peptide helices. The method is based on the comparison of amide and Hα chemical shift changes originated upon the addition of stabilizing or denaturing agents with true helical conformational shifts that have been measured for the first time using an isolated model peptide helix, the one formed by Ac-(Leu-Lys-Lys-Leu)3-NHEt in aqueous solution. © 1990.
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页码：1009 / 1014
页数：6
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