Conservation of amino acids into multiple alignments involved in pairwise interactions in three-dimensional protein structures.
We present an original strategy, that involves a bioinformatic software structure, in order to perform an exhaustive and objective statistical analysis of three-dimensional structures of proteins. We establish the relationship between multiple sequences alignments and various structural features of proteins. We show that amino acids implied in disulfide bonds, salt bridges and hydrophobic interactions have been studied. Furthermore, we point out that the more variable the sequences within a multiple alignment, the more informative the multiple alignment. The results support multiple alignments usefulness for predictions of structural features.
Errami
Mounir
M
Pôle Bioinfomatique Lyonnais-Institute de Biologie et Chimie des Protéines, Laboratoire de Bioinformatique et RMN structurales, Lyon cedex, France. m.errami@ibcp.fr
Geourjon
Christophe
C
Deléage
Gilbert
G
D000595:Amino Acid Sequence; D019295:Computational Biology; D017124:Conserved Sequence; D004220:Disulfides / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D012492:Salts / Q000737:chemistry; D016415:Sequence Alignment / Q000706:statistics & numerical data*; D012984:Software
D004220:Disulfides; D011506:Proteins; D012492:Salts