Protein multiple alignment incorporating primary and secondary structure information.
Identifying common local segments, also called motifs, in multiple protein sequences plays an important role for establishing homology between proteins. Homology is easy to establish when sequences are similar (sharing an identity > 25%). However, for distant proteins, it is much more difficult to align motifs that are not similar in sequences but still share common structures or functions. This paper is a first attempt to align multiple protein sequences using both primary and secondary structure information. A new sequence model is proposed so that the model assigns high probabilities not only to motifs that contain conserved amino acids but also to motifs that present common secondary structures. The proposed method is tested in a structural alignment database BAliBASE. We show that information brought by the predicted secondary structures greatly improves motif identification. A website of this program is available at www.stat.purdue.edu/~junxie/2ndmodel/sov.html.
Kim
Nak-Kyeong
NK
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA.
Xie
Jun
J
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D030562:Databases, Protein; D016013:Likelihood Functions; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012984:Software
D011506:Proteins