Ensemble of transition states for two-state protein folding from the eigenvectors of rate matrices
Ensemble of transition states for two-state protein folding from the eigenvectors of rate matrices
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DOI：
10.1063/1.1802674
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发表时间：
2004-11-08
影响因子：
4.4
通讯作者：
Szabo, A
中科院分区：
文献类型：
--
作者：
Berezhkovskii, A;Szabo, A
研究了描述双态蛋白质折叠过程中微观态相互转换的速率矩阵特征向量的过渡态系综。对应于平衡分布的第一个特征值为0，λ 1= 0，其余为负值。双态蛋白的一个显著特征是特征值谱中存在间隙。研究人员指出，寻找过渡态系综的过程将用于分析两态蛋白质折叠的微观动力学模型，并将对折叠的潜在机制产生有意义的见解。
The transition state ensemble from the eigenvectors of a rate matrix that describes the interconversion of microstates during the folding of a two-state protein was investigated. The first eigenvalue, which corresponds to the equilibrium distribution, is zero, λ 1= 0 and the rest are negative. A distinctive feature of two-state proteins is the presence of a gap in the eigenvalue spectrum. It is stated that the procedure for finding the transition state ensemble will be used to analyze the microscopic kinetics models of two-state protein folding and will lead to meaningful insights into the underlying mechanism of the folding.