Correlation among hydrophobic aromatic and aliphatic residues in the six enzyme classes
by Anindita Roy Chowdhury (Chakravarty); H.G. Nagendra; Alpana Seal
International Journal of Computational Biology and Drug Design (IJCBDD), Vol. 13, No. 2, 2020

Abstract: Hydrophobic force as one of the fundamental forces contributes in folding of the primary sequence of amino acids into a functional three dimensional protein structure. Hydrophobic interactions of side-chains provide maximum stability to correctly folded proteins. Earlier, the authors identified the aromatic and aliphatic residues contributing maximum and minimum hydrophobicity in all the six enzyme classes. The present investigation examines the relative contributions towards hydrophobicity of the different hydrophobic amino acids in both aromatic and aliphatic categories. Notably in a sequence, inverse relationship between residues of similar hydrophobic strength both in aromatic and aliphatic categories seems to exist. This analysis is likely to provide insight for finer analysis of the enzyme molecule.

Online publication date: Wed, 13-May-2020

The full text of this article is only available to individual subscribers or to users at subscribing institutions.

 
Existing subscribers:
Go to Inderscience Online Journals to access the Full Text of this article.

Pay per view:
If you are not a subscriber and you just want to read the full contents of this article, buy online access here.

Complimentary Subscribers, Editors or Members of the Editorial Board of the International Journal of Computational Biology and Drug Design (IJCBDD):
Login with your Inderscience username and password:

Username:        Password:          Forgotten your password?

Want to subscribe?
A subscription gives you complete access to all articles in the current issue, as well as to all articles in the previous three years (where applicable). See our Orders page to subscribe.

If you still need assistance, please email subs@inderscience.com