Relating sequence encoded information to form and function of intrinsically disordered proteins

被引：300

作者：

Das, Rahul K.

Ruff, Kiersten M.

Pappu, Rohit V. ^{[1
]}

机构：

[1] Washington Univ, Dept Biomed Engn, St Louis, MO 63130 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2015年 / 32卷

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

SINGLE-MOLECULE SPECTROSCOPY; MONTE-CARLO SIMULATIONS; NUCLEAR-PORE COMPLEX; INTERNAL-FRICTION; CONFORMATIONAL DYNAMICS; UNFOLDED PROTEINS; ATOMIC-RESOLUTION; AQUEOUS-SOLUTIONS; ENERGY LANDSCAPE; ENSEMBLE;

D O I：

10.1016/j.sbi.2015.03.008

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：

Intrinsically disordered proteins (IDPs) showcase the importance of conformational plasticity and heterogeneity in protein function. We summarize recent advances that connect information encoded in IDP sequences to their conformational properties and functions. We focus on insights obtained through a combination of atomistic simulations and biophysical measurements that are synthesized into a coherent framework using polymer physics theories.

引用

收藏

页码：102 / 112

页数：11

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