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Detection of discriminative sequence motifs in proteins obtained from prokaryotes grown at various temperatures
Author(s) -
Wu LiCheng,
Horng JorngTzong,
Huang ShirLy,
Huang HsienDa,
Liu BawJhiune
Publication year - 2006
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20391
Subject(s) - thermophile , thermostability , discriminative model , subfamily , computational biology , mesophile , biology , multiple sequence alignment , genetics , protein sequencing , sequence (biology) , structural motif , peptide sequence , sequence alignment , biochemistry , gene , computer science , bacteria , enzyme , artificial intelligence
Recent investigations on the stability of proteins have demonstrated various structural factors, but few have considered sequence factors such as protein motifs. These motifs represent highly conserved regions and describe critical regions that may only exist on proteins that remain functional at high temperatures. This investigation presents a method for identifying and comparing corresponding mesophilic and thermophilic sequence motifs between protein families. Discriminative motifs that are conserved only in the mesophilic or thermophilic subfamily are identified. Analysis of the results shows that, although the subfamilies of most protein families share similar motifs, some discriminative motifs are present in particular thermophilic/mesophilic subfamilies. The thermophilic discriminative motifs are conserved only in thermophilic organisms, revealing that physiochemical principles support thermostability. © 2006 Wiley Periodicals, Inc. J Comput Chem 27: 798–808, 2006