QUANTITATIVE-EVALUATION OF INTERPROTON DISTANCES IN PEPTIDES BY 2-DIMENSIONAL OVERHAUSER EFFECT SPECTROSCOPY

被引：21

作者：

SAULITIS, J

LIEPINS, E

机构：

[1] Institute of Organic Synthesis, Latvian Academy of Sciences, Riga, Latvia 226006

来源：

JOURNAL OF MAGNETIC RESONANCE | 1990年 / 87卷 / 01期

关键词：

D O I：

10.1016/0022-2364(90)90087-P

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A quantitative method for the evaluation of interproton distances in peptides in solution was developed. The method is based on the measurement of relative intensities of cross peaks in pure-phase absorption NOESY spectra. The ratio of cross-peak intensities (INα/IαN and INN/IαN) enables one to determine the corresponding interproton distances dNα, dαN, and dNN for several amino acid residues. These distances can be used to estimate other distances having cross peaks in NOESY spectra. For experimental verification interproton distances were determined in a cyclic nonpeptide, namely a cyclic analog of the peptide hormone bradykin. © 1990.

引用

页码：80 / 91

页数：12

共 26 条

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