Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes.
Polypeptides constituting the same functional enzyme in cells of different origins have small sequence similarities among themselves. Amino acid analysis reveals that each glycosyl hydrolase sub-family polypeptides conserves an average hydrophobicity value for total constituent apolar amino acids. The value may be a measure of the driving force present in the polypeptide for designed primary collapse for three-dimensional active site formation.
Sengupta
Subhabrata
S
Department of Biotechnology, Heritage Institute of Technology, Chowbaga Road, Anandapur, East Calcutta Township, Calcutta 700107. India. profs_sengupta@yahoo.ca
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis / Q000737:chemistry*; D001665:Binding Sites; D017124:Conserved Sequence; D006867:Hydrolases / Q000737:chemistry* / Q000145:classification*; D057927:Hydrophobic and Hydrophilic Interactions; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D017510:Protein Folding
D000596:Amino Acids; D010455:Peptides; D006867:Hydrolases