Hydropathy analysis to correlate structure and function of proteins.
In post-genomic era, a plethora of protein structures have been solved but the functions of some of them are unknown. In this context, the role of hydropathy index of amino acids in predicting the function of a structurally known and functionally unknown protein was explored. Initially serine protease class was taken for analysis. Various methodologies like calculation of average hydropathy index for a five-residue window of a given sequence, hydropathy cluster analyses, etc., were done. Among these, the distribution of hydropathy clusters seems to suggest that the location of these clusters is conserved for a given class of proteins. Hence, this methodology was extended to different classes of proteins and to a protein with unknown function.
Damodharan
Lakshminarasimhan
L
Department of Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India.
Pattabhi
Vasantha
V
D000465:Algorithms; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry* / Q000145:classification*; D020539:Sequence Analysis, Protein / Q000379:methods*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D011506:Proteins