The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it
The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it
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DOI：
10.1016/s0301-4622(03)00096-6
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发表时间：
2003-09-01
影响因子：
3.8
通讯作者：
Petsko, GA
中科院分区：
文献类型：
--
作者：
Ringe, D;Petsko, GA
所有的蛋白质在大约200 K的温度下，其动力学性质都会发生剧烈的变化。在此温度以上，它们的动力学行为由键合和非键合原子团的大规模集体运动主导。在较低的温度下，简谐振动占主导地位。这种转变被描述为“玻璃化转变”，以强调单个蛋白质分子的动态行为变化与液体形成玻璃时粘度和其他性质变化之间的某些相似性。玻璃化转变可能反映了蛋白质本身、蛋白质表面上的结合溶剂中原子运动的内在温度依赖性，或者它可能反映了两者的贡献。蛋白质的功能显着改变低于这个转变温度，这一事实可以被利用来捕获酶催化反应中通常不稳定的中间体，并使它们稳定足够长的时间，以允许它们的表征高分辨率蛋白质晶体学。(C)2003 Elsevier Science B.V.保留所有权利。
All proteins undergo a dramatic change in their dynamical properties at approximately 200 K. Above this temperature, their dynamic behavior is dominated by large-scale collective motions of bonded and nonbonded groups of atoms. At lower temperatures, simple harmonic vibrations predominate. The transition has been described as a 'glass transition' to emphasize certain similarities between the change in dynamic behavior of individual protein molecules and the changes in viscosity and other properties of liquids when they form a glass. The glass transition may reflect the intrinsic temperature dependence of the motions of atoms in the protein itself, in the bound solvent on the surface of the protein, or it may reflect contributions from both. Protein function is significantly altered below this transition temperature; a fact that can be exploited to trap normally unstable intermediates in enzyme-catalyzed reactions and stabilize them for periods long enough to permit their characterization by high-resolution protein crystallography. (C) 2003 Elsevier Science B.V. All rights reserved.