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Title: Aromatic-Aromatic Interactions in Biological System: Structure Activity Relationships

While, intramolecular hydrogen bonds have attracted the greatest attention in studies of peptide conformations, the recognition that several other weakly polar interactions may be important determinants of folded structure has been growing. Burley and Petsko provided a comprehensive overview of the importance of weakly polar interactions, in shaping protein structures. The interactions between aromatic rings, which are spatially approximate, have attracted special attention. A survey of the proximal aromatic residue pairs in proteins, allowed Burley and Petsko to suggest that, “phenyl ring centroids are separated by a preferential distance of between 4.5 and 7 Å, and dihedral angles approximately 90° are most common”.
Authors:
;  [1] ;  [2]
  1. Molecular Biophysics Unit, Indian Institute of Sciences-Bangalore, Karnataka (India)
  2. Bio-Spatial Technology Research Unit, Department of Environmental Biotechnology, School of Environmental Sciences, Bharathidasan University, Tiruchirappalli, Tamil Nadu (India)
Publication Date:
OSTI Identifier:
22504545
Resource Type:
Journal Article
Resource Relation:
Journal Name: Research and Reviews: Journal of Chemistry; Journal Volume: 5; Journal Issue: 1; Other Information: Copyright: (c) 2016 Rajagopal Appavu; This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
India
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; HYDROGEN; INTERACTIONS; PEPTIDES; RESIDUES; STRUCTURE-ACTIVITY RELATIONSHIPS