title: Computational analysis of N-H⋯π interactions and its impact on the structural stability of β-lactamases.
abstract: Studies on intra-protein interactions provide valuable information on protein conformation. The aim of our study is to explore the functional importance of residues participating in N-H⋯π hydrogen bonds in maintaining the conformational stability of β-lactamases. Our results show that most of the residues participating in N-H⋯π hydrogen bond formation are functionally important and play a significant role in stabilizing the structure with more than one stabilizing region. Our findings reveal the importance of N-H⋯π hydrogen bonds in the stability of β-lactamases. These findings may be helpful for medicinal and computational protein chemists working in the area of enzyme mediated antibiotic resistance.
authors: Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors: P
authors: P
authors: Lavanya
authors: Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
authors: Sudha
authors: S
authors: Ramaiah
authors: Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India. Electronic address: aanand@vit.ac.in.
authors: Anand
authors: A
authors: Anbarasu
mesh_terms: D004795:Enzyme Stability; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D001618:beta-Lactamases / Q000737:chemistry*
chemical_list: D001618:beta-Lactamases
keywords: Conservation; N–H⋯π hydrogen bonds; Secondary structure; Solvent accessibility; Stabilization centers; β-lactamases