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

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 0.24 Å for the peptide's backbone atoms and 0.65 Å for all non-hydrogen atoms.

Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (122 K)Download as PowerPoint slideHighlights► We performed molecular dynamics folding simulation of a choline-binding peptide. ► An unbiased selection of a representative folded-state structure was performed. ► The agreement between experiment and simulation was outstandingly accurate.