Authors: Anindita Roy Chowdhury (Chakravarty); H.G. Nagendra; Alpana Seal
Addresses: 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, India
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.
Keywords: hydrophobicity scale; enzymes; correlation between hydrophobic residues; residual plot; inverse relation.
International Journal of Computational Biology and Drug Design, 2020 Vol.13 No.2, pp.209 - 223
Accepted: 20 Aug 2019
Published online: 10 May 2020 *