Anand anbarasu

P s shrivaishnavi

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Role of Cation-π Interactions in the Structural Stability of Bacterial Exotoxins

Journal of Microbial & Biochemical Technology

p-p Interactions play an important role in the stability of protein structures. In the present study, we have analyzed the influence of p-p interactions in eNOS and nNOS proteins. The contribution of these p-p interacting residues in sequential separation, secondary structure involvement, solvent accessibility and stabilization centers has been evaluated. p-p interactions stabilize the core regions within eNOS and nNOS proteins. p-p interacting residues are evolutionary conserved. There is a significant number of p-p interactions in spite of the lesser natural occurrences of p-residues in eNOS and nNOS proteins. In addition to p-p interactions, presidues also form p-p networks in both eNOS and nNOS proteins which might play an important role in the structural stability of these protein structures. © 2013 Elsevier Inc. All rights reserved.

Bioorganic Chemistry

Investigations on the role of π–π interactions and π–π networks in eNOS and nNOS proteins

β-lactam group of antibiotics is the most widely used therapeutic molecules for treating bacterial infections. The main mode of bacterial resistance to β-lactams is by β-lactamases. In the present study, we report our results on the role of cation-π interactions in β-lactamases and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while tyrosine is comparatively higher than phenylalanine and tryptophan in the π group. Our results indicate that cation-π interactions might play an important role in the global conformational stability of β-lactamases.

Journal	Journal of Microbial & Biochemical Technology
Publisher	OMICS Publishing Group
Open Access	0