Interplay between peptide bond geometrical parameters in nonglobular structural contexts(463 views) Esposito L, Balasco N, De Simone A, Berisio R, Vitagliano L
Biomed Res Int (ISSN: 2314-6133, 2314-6141, 2314-6141electronic), 2013; 2013: N/D-N/D.
Keywords: Amyloid, Collagen, Collagen Like Peptide, Globular Protein, Membrane Protein, Unclassified Drug, Water Soluble Protein, Amyloid Protein, Article, Geometry, Protein Binding, Protein Conformation, Protein Function, Protein Stability, Protein Structure, Triple Helix, Chemical Structure, Chemistry, Hydrogen Bond, Protein Secondary Structure, Amyloidogenic Proteins, Hydrogen Bonding, Models, Molecular, Amyloidogenic Proteins Chemistry, Collagen Chemistry, Water Chemistry,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Seconda Università di Napoli, Via Vivaldi 43, 81100 Caserta, Italy
Division of Molecular Biosciences, Imperial College South Kensington Campus, London SW7 2AZ, United Kingdom
Seconda Universita di Napoli, Via Vivaldi 43, 81100 Caserta, Italy.
Seconda Universit di Napoli, Via Vivaldi 43, 81100 Caserta, Italy
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Interplay between peptide bond geometrical parameters in nonglobular structural contexts
Several investigations performed in the last two decades have unveiled that geometrical parameters of protein backbone show a remarkable variability. Although these studies have provided interesting insights into one of the basic aspects of protein structure, they have been conducted on globular and water-soluble proteins. We report here a detailed analysis of backbone geometrical parameters in nonglobular proteins/peptides. We considered membrane proteins and two distinct fibrous systems (amyloid-forming and collagen-like peptides). Present data show that in these systems the local conformation plays a major role in dictating the amplitude of the bond angle N-C(alpha)-C and the propensity of the peptide bond to adopt planar/nonplanar states. Since the trends detected here are in line with the concept of the mutual influence of local geometry and conformation previously established for globular and water-soluble proteins, our analysis demonstrates that the interplay of backbone geometrical parameters is an intrinsic and general property of protein/peptide structures that is preserved also in nonglobular contexts. For amyloid-forming peptides significant distortions of the N-C(alpha)-C bond angle, indicative of sterical hidden strain, may occur in correspondence with side chain interdigitation. The correlation between the dihedral angles Deltaomega/psi in collagen-like models may have interesting implications for triple helix stability.
Interplay between peptide bond geometrical parameters in nonglobular structural contexts
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