Title
Search for conserved amino acid residues of the α-crystallin proteins of vertebrates.
Abstract
α-crystallin is the major eye lens protein and a member of the small heat-shock protein (sHsp) family. α-crystallins have been shown to support lens clarity by preventing the aggregation of lens proteins. We performed the bioinformatics analysis of α-crystallin sequences from vertebrates to find conserved amino acid residues as the three-dimensional (3D) structure of α-crystallin is not identified yet. We are the first who demonstrated that the N-terminal region is conservative along with the central domain for vertebrate organisms. We have found that there is correlation between the conserved and structured regions. Moreover, amyloidogenic regions also correspond to the structured regions. We analyzed the amino acid composition of α-crystallin A and B chains. Analyzing the occurrence of each individual amino acid residue, we have found that such amino acid residues as leucine, serine, lysine, proline, phenylalanine, histidine, isoleucine, glutamic acid, and valine change their content simultaneously in A...
Year
Venue
Field
2016
J. Bioinformatics and Computational Biology
Conserved sequence,Lens protein,Biology,Crystallin,Biochemistry,Amino acid,Leucine,Valine,Alpha-Crystallins,Bioinformatics,Peptide sequence
DocType
Volume
Issue
Journal
14
2
Citations 
PageRank 
References 
1
0.37
4
Authors
3
Name
Order
Citations
PageRank
Nikita G. Shiliaev110.37
Olga M. Selivanova210.37
Oxana V. Galzitskaya312520.15