DOI: 10.5176/2251-2489_ BioTech14.28
Authors: Akshay Bhatnagar and Debashree Bandyopadhyay
Abstract: Three dimensional spatial arrangements of hydrophilic and hydrophobic functional groups constitute the micro-environment around an amino acid within a protein structure. This micro-environment strongly influences various structure and functional aspects of that particular amino acid which, in turn, contribute to the overall structure and function of the protein. Here we have exploited the micro-environment database, generated for Cystine disulphide-bridged residues in the context of high-resolution crystal structure, to understand the implicit relationship between micro-environment and the functional aspects of that particular Cystine residue embedded in the micro-environment. Individual residue functions are curated from the large literature database. Following rules are being deduced from this study regarding the Cystine residue function and its implication in protein structure. i) Disulphide linked Cystine residues are mainly involved in structural stabilization via formation of intra and inter chain disulphide bond. ii) Cystine residues participate in protein function only via formation of few structural motifs and iii) by participating in the protein active site. iv) Unlike the hydrophilic residues, Cystine residue is in functional form only when it is deeply buried inside a protein structure.
Keywords: Protein micro-environment, high-resolution crystal structure, buried fraction, rHpy, micro-environment space, oxidized Cystine, reduced Cystine, structural rules, SCOP classes, normalized occupancies, text-mining
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