Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes.

Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes. Research Abstract Details 

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Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes. Abstract Text:

Subhabrata Sengupta,Subhabrata Sengupta,Subhabrata Sengupta,

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.

Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes. Publishing Authors By Initials

S Sengupta,S Sengupta,S Sengupta,

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Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Protein and peptide letters

VOLUME: 14

Page Numbers: 843-5

Journal Abbreviation: Protein Pept. Lett.

ISSN: 0929-8665

DAY: 29

MONTH: 11

YEAR: 2007

Conservation of average hydrophobicity of apolar aminoacids in polypeptides constituting same glycosyl hydrolase sub-family enzymes. Information

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LANGUAGE: eng

NlmUniqueID: 9441434

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AFFILIATION: Department of Biotechnology, Heritage Institute of Technology, Chowbaga Road, Anandapur, East Calcutta Township, Calcutta 700107. India. profs_sengupta@yahoo.ca.

Country: Netherlands

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MEDLINETA: Protein Pept Lett

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