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蛋白质结构转变的统计力学:来自岛屿模型的见解。

Statistical mechanics of protein structural transitions: Insights from the island model.

作者信息

Kobayashi Yukio

机构信息

Department of Information Systems Science, Faculty of Science and Engineering, Soka Univeristy, Hachioji, Tokyo 192-8577, Japan.

出版信息

Biophys Physicobiol. 2016 Nov 18;13:251-262. doi: 10.2142/biophysico.13.0_251. eCollection 2016.

DOI:10.2142/biophysico.13.0_251
PMID:28409078
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5221510/
Abstract

The so-called island model of protein structural transition holds that hydrophobic interactions are the key to both the folding and function of proteins. Herein, the genesis and statistical mechanical basis of the island model of transitions are reviewed, by presenting the results of simulations of such transitions. Elucidating the physicochemical mechanism of protein structural formation is the foundation for understanding the hierarchical structure of life at the microscopic level. Based on the results obtained to date using the island model, remaining problems and future work in the field of protein structures are discussed, referencing Professor Saitô's views on the hierarchic structure of science.

摘要

所谓的蛋白质结构转变的岛状模型认为,疏水相互作用是蛋白质折叠和功能的关键。本文通过展示此类转变的模拟结果,对转变的岛状模型的起源和统计力学基础进行了综述。阐明蛋白质结构形成的物理化学机制是在微观层面理解生命层次结构的基础。基于迄今为止使用岛状模型获得的结果,参考斋藤教授关于科学层次结构的观点,讨论了蛋白质结构领域中尚存的问题和未来的工作。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b435/5221510/ca1d9ea488f6/13_251f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b435/5221510/63b4a696a848/13_251f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b435/5221510/ca1d9ea488f6/13_251f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b435/5221510/63b4a696a848/13_251f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b435/5221510/ca1d9ea488f6/13_251f2.jpg

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引用本文的文献

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Memorial Issue for Professor Nobuhiko Saitô.纪念斋藤信彦教授专刊。
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本文引用的文献

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Intramolecular alpha-helix-beta-structure-random coil transition in polypeptides. II. Dynamic case.多肽分子内α-螺旋-β-结构-无规卷曲转变。II. 动态情况。
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