通过φ值与残基间接触的相关性分析胰凝乳蛋白酶抑制剂的折叠途径。
Analysis of the folding pathway of chymotrypsin inhibitor by correlation of phi-values with inter-residue contacts.
作者信息
Nolting B
机构信息
Prussian Private Institute of Technology at Berlin, Gorschstrasse 40, D-13187 Berlin, Germany.
出版信息
J Theor Biol. 1999 Mar 7;197(1):113-21. doi: 10.1006/jtbi.1998.0860.
The transition state for folding of chymotrypsin inhibitor 2 (CI2) is investigated by correlating Phi-values with inter-residue contacts. In agreement with former work, the strongest consolidation of secondary structure is found in the alpha-helix. There are correlations for tertiary structure interactions between the residues Leu49, Ile57 and the helix which have been suggested to represent the main components of the nucleation site of CI2 folding. However, correlations for tertiary structure interactions of comparable magnitude are also found in the helix-strand2-strand1-motif and between strand3and strand4. Copyright 1999 Academic Press.
通过将φ值与残基间接触进行关联，研究了胰凝乳蛋白酶抑制剂2（CI2）折叠的过渡态。与之前的工作一致，在α螺旋中发现二级结构的最强巩固。残基Leu49、Ile57与螺旋之间存在三级结构相互作用的相关性，这些相互作用被认为代表了CI2折叠成核位点的主要成分。然而，在螺旋-链2-链1基序以及链3和链4之间也发现了具有相当程度的三级结构相互作用的相关性。版权所有1999年学术出版社。
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