Intramolecular Distance Distribution Reveals Mechanisms in Protein Folding and Dynamics

被引：1

作者：

Krishnamoorthy, G. ^{[1
,2
]}

机构：

[1] Anna Univ, Dept Biotechnol, Madras 600025, Tamil Nadu, India

[2] Indian Inst Technol, Dept Chem, Bombay 400076, Maharashtra, India

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES INDIA SECTION A-PHYSICAL SCIENCES | 2018年 / 88卷 / 03期

关键词：

Structural heterogeneity; Fluorescence lifetime distribution; Maximum entropy method; Protein folding; Molecular crowding; FLUORESCENCE LIFETIME DISTRIBUTIONS; MAXIMUM-ENTROPY METHOD; MOTIONAL DYNAMICS; TRANSITIONS; BARSTAR; DOMAIN; STATE; MODEL;

D O I：

10.1007/s40010-018-0525-3

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Flexibility and dynamics in polypeptides and proteins give rise to conformational and structural heterogeneity. Quantification of the level of heterogeneity is essential for providing deeper understanding of molecular mechanisms in protein folding. Fluorescence lifetime distribution generated by the maximum entropy method (MEM) provides an unbiased estimate of intramolecular distance distribution. This article discusses several examples where MEM-generated lifetime distribution brings out site-specific conformational and structural heterogeneity in proteins. Use of the information on intamolecular distance distribution in revealing molecular mechanisms of protein folding is also discussed.

引用

页码：415 / 424

页数：10

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