BibTeX
@MISC{Rost99twilightzone,
author = {Burkhard Rost},
title = {Twilight Zone of Protein Sequence Alignments},
year = {1999}
}
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Abstract
l findings are applicable to automatic database searches. Keywords: alignment quality analysis/evolutionary conservation/ genome analysis/protein sequence alignment/sequence space hopping Introduction Protein sequence alignments in twilight zone Protein sequences fold into unique three-dimensional (3D) structures. However, proteins with similar sequences adopt similar structures (Zuckerkandl and Pauling, 1965; Doolittle, 1981; Doolittle, 1986; Chothia and Lesk, 1986). Indeed, most protein pairs with more than 30 out of 100 identical residues were found to be structurally similar (Sander and Schneider, 1991). This high robustness of structures with respect to residue exchanges explains partly the robustness of organisms with respect to gene-replication errors, and it allows for the variety in evolution (Zuckerkandl and Pauling, 1965; Zuckerkandl, 1976; Doolittle, 1979, 1986). Structure alignments have uncovered homologous protein pairs with less than 10% pairwise sequence identity (
Keyphrases
twilight zone protein sequence alignment high robustness protein pair identical residue twilight zone protein automatic database search gene-replication error similar sequence similar structure structure alignment introduction protein sequence alignment homologous protein pairwise sequence identity
