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

Subhabrata      Sengupta

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