CONFORMATIONAL PREFERENCES OF OLIGOPEPTIDES RICH IN ALPHA-AMINOISOBUTYRIC-ACID .2. A MODEL FOR THE 310/ ALPHA-HELIX TRANSITION WITH COMPOSITION AND SEQUENCE SENSITIVITY

被引：44

作者：

BASU, G

KUKI, A

机构：

[1] Cornell University, Department of Chemistry, Baker Laboratory, Ithaca, New York

来源：

BIOPOLYMERS | 1992年 / 32卷 / 01期

关键词：

D O I：

10.1002/bip.360320109

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The analysis of the factors that control the helical folding of Aib-rich peptides is extended to include sensitivity to sequence patterns, and in particular the presence of contiguous non-Aib alpha-mono-alkylated residues. The distinct hydrogen-bonding network of the 3(10)-helix, as contrasted with that of the competing alpha-helical structure, is explicitly incorporated into a theoretical model for the 3(10)-helix/alpha-helix equilibrium constant for a given peptide. Finite length effects and the "extra" intrahelical hydrogen bond of the 3(10) form are expressed naturally as a result of this loop analysis. This semiempirical model captures all the established features of existing empirical rules for helical conformational transitions in Aib-rich sequences, as well as the recently detected helical transition induced solely by sequence permutation.

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页码：61 / 71

页数：11

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