细胞内及拥挤环境下体外的蛋白质复合物稳定性。
Protein-complex stability in cells and in vitro under crowded conditions.
机构信息
Department of Chemistry, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599-3290, USA.
Department of Chemistry, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599-3290, USA; Department of Biochemistry and Biophysics, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599, USA; Integrative Program for Biological and Genome Sciences, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599, USA.
出版信息
Curr Opin Struct Biol. 2021 Feb;66:183-192. doi: 10.1016/j.sbi.2020.10.024. Epub 2020 Dec 4.
Biology is beginning to appreciate the effects of the crowded and complex intracellular environment on the equilibrium thermodynamics and kinetics of protein folding. The next logical step involves the interactions between proteins. We review quantitative, wet-experiment based efforts aimed at understanding how and why high concentrations of small molecules, synthetic polymers, biologically relevant cosolutes and the interior of living cells affect the energetics of protein-protein interactions. We then address popular theories used to explain the effects and suggest expeditious paths for a more methodical integration of experiment and simulation.
生物学开始认识到拥挤而复杂的细胞内环境对蛋白质折叠的平衡热力学和动力学的影响。下一步涉及蛋白质之间的相互作用。我们回顾了旨在理解小分子、合成聚合物、生物相关共溶剂和活细胞内部的高浓度如何以及为什么影响蛋白质-蛋白质相互作用的能量学的定量、基于实验的努力。然后，我们讨论了用于解释这些影响的流行理论，并为更系统地将实验和模拟结合起来提出了快捷途径。
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