期刊
BIOESSAYS
卷 32, 期 8, 页码 655-658出版社
JOHN WILEY & SONS INC
DOI: 10.1002/bies.201000038
关键词
fitness; mutation; protein folding; split beta-lactamase assay; stability-function tradeoff
资金
- National Science Foundation [MCB-0749836]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0749836] Funding Source: National Science Foundation
A new split beta-lactamase assay promises experimental testing of the interplay of protein stability and function. Proteins are sufficiently stable to act effectively within cells. However, mutations generally destabilize structure, with effects on free energy that are comparable to the free energy of folding. Assays of protein functionality and stability in vivo enable a quick study of factors that influence these properties in response to targeted mutations. These assays can help molecular engineering but can also be used to target important questions, including why most proteins are marginally stable, how mutations alter structural makeup, and how thermodynamics, function, and environment shape molecular change. Processes of self-organization and natural selection are determinants of stability and function. Non-equilibrium thermodynamics provides crucial concepts, e.g., cells as emergent energy-dissipating entities that do work and build their own parts, and a framework to study the sculpting role of evolution at different scales.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据