Exploring Regions of Conformational Space Occupied by Two-Domain Proteins

被引：24
作者：
Andralojc, Witold [1 ,2 ]
Luchinat, Claudio [1 ,2 ]
Parigi, Giacomo [1 ,2 ]
Ravera, Enrico [1 ,2 ]
机构：
[1] Univ Florence, Ctr Magnet Resonance, I-50019 Sesto Fiorentino, Italy
[2] Univ Florence, Dept Chem Ugo Schiff, I-50019 Sesto Fiorentino, Italy
来源：
JOURNAL OF PHYSICAL CHEMISTRY B | 2014年 / 118卷 / 36期
关键词：
PARAMAGNETIC RELAXATION ENHANCEMENT; RESIDUAL DIPOLAR COUPLINGS; X-RAY; NMR-SPECTROSCOPY; RNA DYNAMICS; DOMAIN; ENSEMBLES; TRANSIENT; STATES; HETEROGENEITY;
D O I：
10.1021/jp504820w
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The presence of heterogeneity in the interdomain arrangement of several biomolecules is required for their function. Here we present a method to obtain crucial clues to distinguish between different kinds of protein conformational distributions based on experimental NMR data. The method explores subregions of the conformational space and provides both upper and lower bounds of probability for the system to be in each subregion.
引用
收藏
页码：10576 / 10587
页数：12
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