Multicanonical simulation of coupled folding and binding of intrinsically disordered protein using an Ising-like protein model

24th IUPAP Conference on Computational Physics

物理学;计算机科学

Matsushita, Katsuyoshi^1,2 ; Kikuchi, MacOto^1,3,4

Cybermedia Center, Osaka University, Toyonaka 560-0032, Japan^1

Institute for Protein Research, Osaka University, 565-0871, Suita, Japan^2

Graduate School of Science, Osaka University, Toyonaka 643-0043, Japan^3

Graduate School of Frontier Biosciences, Osaka University, 565-0871, Suita, Japan^4

关键词: Computational biophysics;    Energy-entropy;    Free energy landscape;    Intrinsically disordered proteins;    Multicanonical simulations;    Physiological condition;    Protein modeling;    Target proteins;   

Others  :  https://iopscience.iop.org/article/10.1088/1742-6596/454/1/012034/pdf
DOI  :  10.1088/1742-6596/454/1/012034

学科分类：计算机科学（综合）

来源: IOP

【 摘 要 】

An intrinsically disordered protein is one that does not spontaneously fold in physiological conditions but only folds when it binds to a target protein. Computer simulation of this coupled folding and binding is one of the central subjects of computational biophysics. Computing the free energy landscape is helpful in understanding coupled folding and binding. For this reason, we developed an Ising-like protein model and a multicanonical simulation in an energy-entropy space. The calculated free energy landscape indicates that coupled folding and binding induces rapid structural switching of the bound target protein.