Conservation of Average Hydrophobicity of Apolar Aminoacids in Polypeptides Constituting Same Glycosyl Hydrolase Sub-Family Enzymes

Subhabrata      Sengupta

doi:10.2174/092986607782110284

Abstract

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.

Keywords: Glycosyl hydrolase, apolar aminoacid hydrophobicity, protein folding, protein hydrophobicity

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Protein & Peptide Letters

Title: Conservation of Average Hydrophobicity of Apolar Aminoacids in Polypeptides Constituting Same Glycosyl Hydrolase Sub-Family Enzymes

Volume: 14 Issue: 9

Author(s): Subhabrata Sengupta

Affiliation:

Keywords: Glycosyl hydrolase, apolar aminoacid hydrophobicity, protein folding, protein hydrophobicity

Abstract: 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.

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Sengupta Subhabrata, Conservation of Average Hydrophobicity of Apolar Aminoacids in Polypeptides Constituting Same Glycosyl Hydrolase Sub-Family Enzymes, Protein & Peptide Letters 2007; 14 (9) . https://dx.doi.org/10.2174/092986607782110284