Linking computation and experiments to study the role of charge-charge interactions in protein folding and stability

被引：8
作者：
Makhatadze, George I. [1 ,2 ,3 ]
机构：
[1] Rensselaer Polytech Inst, Ctr Biotechnol & Interdisciplinary Studies, 110 8th St, Troy, NY 12180 USA
[2] Rensselaer Polytech Inst, Dept Biol, 110 8th St, Troy, NY 12180 USA
[3] Rensselaer Polytech Inst, Dept Chem & Chem Biol, Troy, NY 12180 USA
来源：
PHYSICAL BIOLOGY | 2017年 / 14卷 / 01期
基金：
美国国家科学基金会;
关键词：
protein folding; charge-charge interactions; protein stability; COLD SHOCK PROTEIN; SINGLE-STRANDED-DNA; INTRINSICALLY DISORDERED PROTEINS; TRANSITION-STATE ENSEMBLE; MONTE-CARLO SIMULATION; HELICAL COILED-COILS; ELECTROSTATIC INTERACTIONS; GLOBULAR-PROTEINS; ENERGY LANDSCAPE; TOPOLOGICAL FRUSTRATION;
D O I：
10.1088/1478-3975/14/1/013002
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：
Over the past two decades there has been an increase in appreciation for the role of surface charge-charge interactions in protein folding and stability. The perception shifted from the belief that charge-charge interactions are not important for protein folding and stability to the near quantitative understanding of how these interactions shape the folding energy landscape. This led to the ability of computational approaches to rationally redesign surface charge-charge interactions to modulate thermodynamic properties of proteins. Here we summarize our progress in understanding the role of charge-charge interactions for protein stability using examples drawn from my own laboratory and touch upon unanswered questions.
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页数：6
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