Metastability of Native Proteins and the Phenomenon of Amyloid Formation
Metastability of Native Proteins and the Phenomenon of Amyloid Formation
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DOI：
10.1021/ja2017703
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发表时间：
2011-09-14
影响因子：
15
通讯作者：
Dobson, Christopher M.
中科院分区：
文献类型：
--
作者：
Baldwin, Andrew J.;Knowles, Tuomas P. J.;Dobson, Christopher M.
一系列淀粉样蛋白原纤维的热力学稳定性的实验测定表明，这种结构形式可能是蛋白质分子即使在生理条件下也能采用的最稳定的结构形式。这一结果挑战了传统的假设，即蛋白质的功能形式对应于其自由能表面的全局最小值，并表明生命系统是构象以及化学亚稳态。
An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions. This result challenges the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces and suggests that living systems are conformationally as well as chemically metastable.