title: As good as it gets? Folding molecular dynamics simulations of the LytA choline-binding peptide result to an exceptionally accurate model of the peptide structure.
abstract: Folding simulations of a choline-binding peptide derived from the Streptococcus pneumoniae LytA protein converged to a model of the peptide's folded state structure which is in outstanding agreement with the experimentally-determined structures, reaching values for the root mean squared deviation as low as 0.24Å for the peptide's backbone atoms and 0.65Å for all non-hydrogen atoms.
authors.affiliation: Department of Molecular Biology and Genetics, Democritus University of Thrace, University Campus, 68100 Alexandroupolis, Greece.
authors.forename: Ilias
authors.initials: I
authors.lastname: Patmanidis
authors.forename: Nicholas M
authors.initials: NM
authors.lastname: Glykos
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D002794:Choline / Q000737:chemistry*; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D025341:Principal Component Analysis; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013296:Streptococcus pneumoniae / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D002794:Choline