Correlation between ω and ψ Dihedral Angles in Protein Structures
Autor: | Luigi Vitagliano, Luciana Esposito, Adriana Zagari, Alfonso De Simone |
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Přispěvatelé: | Esposito, L., De Simone, A., Zagari, A., Vitagliano, L., DE SIMONE, A., Zagari, Adriana |
Rok vydání: | 2005 |
Předmět: |
Models
Molecular Protein Structures Protein geometry-conformation Protein Conformation Statistics as Topic Statistical analyse Dihedral angle Omega dihedral angle Quantitative Biology::Subcellular Processes Protein structure Structural Biology 310 helix Peptide bond Databases Protein Molecular Biology Quantitative Biology::Biomolecules Molecular Structure Chemistry Peptide group planarity Peptide plane flipping dihedral angles Planarity testing Crystallography Vicinal Ramachandran plot |
Zdroj: | Journal of Molecular Biology 2005 (2005): 483–487. doi:10.1016/j.jmb.2005.01.065 info:cnr-pdr/source/autori:Esposito, Luciana; De Simone, Alfonso; Zagari, Adriana; Vitagliano, Luigi./titolo:Correlation between Omega and Psi Dihedral Angles in Protein Structures/doi:10.1016%2Fj.jmb.2005.01.065/rivista:Journal of Molecular Biology/anno:2005/pagina_da:483/pagina_a:487/intervallo_pagine:483–487/volume:2005 |
ISSN: | 0022-2836 |
DOI: | 10.1016/j.jmb.2005.01.065 |
Popis: | The planarity of the peptide group is one of the fundamental features of protein structure that is described in every chemistry and biochemistry textbook. By surveying a dataset of 163 atomic resolution protein structures we here identify the stereochemical conditions that favor significant deformations of peptide bond planarity. In particular, we demonstrate that the values of the ω dihedral angle are strictly correlated to the values of the adjacent ψ angle. This trend is also observed in highly strained states such as those occurring in vicinal disulfide bridges. These findings provide direct evidence for the mutual influence of the geometrical parameters that describe the protein structure. © 2005 Elsevier Ltd. All rights reserved. |
Databáze: | OpenAIRE |
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