Sequencing of folding events in Go-type proteins
Sequencing of folding events in Go-type proteins
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DOI：
10.1063/1.1314868
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发表时间：
2000-11-08
影响因子：
4.4
通讯作者：
Cieplak, M
中科院分区：
文献类型：
--
作者：
Hoang, TX;Cieplak, M
我们研究了三个小的球状蛋白质：crambin，糜蛋白酶抑制剂2（CI 2），和fyn Src同源3域（SH 3）的折叠机制，这是由一个Go型哈密顿与Lennard-Jones相互作用建模。它示出，折叠是由一个明确定义的序列的事件所确定的建立特定的接触。事件的顺序主要取决于原生状态的几何形状。温度、耦合强度和粘度的变化在相当小的程度上影响测序方案。测序与沿着序列的接触氨基酸的距离沿着密切相关。因此，阿尔法螺旋首先建立。Crambin被发现表现得像一个单一的路线文件夹，而在CI 2和SH 3的折叠轨迹更加多样化。CI 2和SH 3的折叠方案与其过渡态的实验研究一致。(C)2000年美国物理学会。[S0021-9606（00）50442-5]。
We have studied folding mechanisms of three small globular proteins: crambin, chymotrypsin inhibitor 2 (CI2), and the fyn Src Homology 3 domain (SH3) which are modeled by a Go-type Hamiltonian with the Lennard-Jones interactions. It is shown that folding is dominated by a well-defined sequencing of events as determined by establishment of particular contacts. The order of events depends primarily on the geometry of the native state. Variations in temperature, coupling strengths, and viscosity affect the sequencing scenarios to a rather small extent. The sequencing is strongly correlated with the distance of the contacting amino acids along the sequence. Thus alpha helices get established first. Crambin is found to behave like a single-route folder, whereas in CI2 and SH3 the folding trajectories are more diversified. The folding scenarios for CI2 and SH3 are consistent with experimental studies of their transition states. (C) 2000 American Institute of Physics. [S0021-9606(00)50442-5].