TY - JOUR
T1 - Analysis of chameleon sequences and their implications in biological processes
AU - Guo, Jun Tao
AU - Jaromczyk, Jerzy W.
AU - Xu, Ying
PY - 2007/5/15
Y1 - 2007/5/15
N2 - 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.
AB - 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.
KW - Alternative splicing
KW - Amyloid fibril
KW - Amyloidosis
KW - Chameleon-he
KW - Chameleon-hs
KW - Isoforms
KW - Molecular dynamics simulations
KW - Secondary structure
UR - https://www.scopus.com/pages/publications/34247223063
UR - https://www.scopus.com/inward/citedby.url?scp=34247223063&partnerID=8YFLogxK
U2 - 10.1002/prot.21285
DO - 10.1002/prot.21285
M3 - Article
C2 - 17299764
AN - SCOPUS:34247223063
SN - 0887-3585
VL - 67
SP - 548
EP - 558
JO - Proteins: Structure, Function and Genetics
JF - Proteins: Structure, Function and Genetics
IS - 3
ER -