Earlier, the authors identified the aromatic and aliphatic residues contributing maximum and minimum hydrophobicity in all the six enzyme classes. Hydrophobic interactions of side-chains provide maximum stability to correctly folded proteins. Nagendra Alpana SealĪddresses: Department of Physics, School of Basic and Applied Sciences, GD Goenka University, Sohna Gurgaon Road, Gurgaon, Haryana – 122103, India ' Department of Biotechnology, Sir M Visvesvaraya Institute of Technology, Bengaluru, Karnataka – 562157, India ' Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, 741235, West Bengal, IndiaĪbstract: 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. Title: Correlation among hydrophobic aromatic and aliphatic residues in the six enzyme classesĪuthors: Anindita Roy Chowdhury (Chakravarty) H.G. International Journal of Computational Biology and Drug Design.Inderscience Publishers - linking academia, business and industry through research This analysis is likely to provide insight for finer analysis of the enzyme molecule.
Notably in a sequence, inverse relationship between residues of similar hydrophobic strength both in aromatic and aliphatic categories seems to exist. The present investigation examines the relative contributions towards hydrophobicity of the different hydrophobic amino acids in both aromatic and aliphatic categories. Article: Correlation among hydrophobic aromatic and aliphatic residues in the six enzyme classes Journal: International Journal of Computational Biology and Drug Design (IJCBDD) 2020 Vol.13 No.2 pp.209 - 223 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.
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