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Acyl carrier protein structural classification and normal mode analysis
Author(s) -
Cantu David C.,
Forrester Michael J.,
Charov Katherine,
Reilly Peter J.
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2050
Subject(s) - protein tertiary structure , protein primary structure , similarity (geometry) , sequence (biology) , protein structure , crystallography , structural similarity , amino acid , peptide sequence , biology , chemistry , computational biology , genetics , biochemistry , computer science , gene , artificial intelligence , image (mathematics)
All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well.