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

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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

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607782110284

Publication date: September 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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