標題: Computation of conformational entropy from protein sequences using the machine-learning method - Application to the study of the relationship between structural conservation and local structural stability
作者: Huang, SW
Hwang, JK
生物科技學系
生物資訊及系統生物研究所
Department of Biological Science and Technology
Institude of Bioinformatics and Systems Biology
關鍵字: structural conservation;sequence structural entropy;structural profile;support vector machines;hydrogen exchange
公開日期: 1-六月-2005
摘要: A complete protein sequence can usually determine a unique conformation; however, the situation is different for shorter subsequences-some of them are able to adopt unique conformations, independent of context; while others assume diverse conformations in different contexts. The conformations of subsequences are determined by the interplay between local and nonlocal interactions. A quantitative measure of such structural conservation or variability will be useful in the understanding of the sequence-structure relationship. In this report, we developed an approach using the support vector machine method to compute the conformational. variability directly from sequences, which is referred to as the sequence structural entropy. As a practical application, we studied the relationship between sequence structural entropy and the hydrogen exchange for a set of well-studied proteins. We found that the slowest exchange cores usually comprise amino acids of the lowest sequence structural entropy. Our results indicate that structural conservation is closely related to the local structural stability. This relationship may have interesting implications in the protein folding processes, and may be useful in the study of the sequence-structure relationship. (c) 2005 Wiley-Liss, Inc.
URI: http://dx.doi.org/10.1002/prot.20462
http://hdl.handle.net/11536/13602
ISSN: 0887-3585
DOI: 10.1002/prot.20462
期刊: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume: 59
Issue: 4
起始頁: 802
結束頁: 809
顯示於類別:期刊論文


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  1. 000229226500014.pdf