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Analysis of chameleon sequences and their implications in biological processes
Author(s) -
Guo JunTao,
Jaromczyk Jerzy W.,
Xu Ying
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21285
Subject(s) - gene isoform , functional diversity , sequence (biology) , computational biology , biology , protein secondary structure , helix (gastropod) , evolutionary biology , sequence analysis , conserved sequence , genetics , peptide sequence , zoology , biochemistry , ecology , gene , gastropoda
Chameleon sequences have been implicated in amyloid related diseases. Here we report an analysis of two types of chameleon sequences, chameleon‐HS (Helix vs. Strand) and chameleon‐HE (Helix vs. Sheet), based on known structures in Protein Data Bank. Our survey shows that the longest chameleon‐HS is eight residues while the longest chameleon‐HE is seven residues. We have done a detailed analysis on the local and global environment that might contribute to the unique conformation of a chameleon sequence. We found that the existence of chameleon sequences does not present a problem for secondary structure prediction programs, including the first generation prediction programs, such as Chou–Fasman algorithm, and the third generation prediction programs that utilize evolution information. We have also investigated the possible implication of chameleon sequences in structural conservation and functional diversity of alternatively spliced protein isoforms. Proteins 2007. © 2007 Wiley‐Liss, Inc.