Angewandte Chemie International Edition · 1999 · 2K citations · 0 references
Life SciencesBiochemistryBiophysicsProtein FoldingStructural BiochemistryStructural BiologyMacromolecular FoldingMolecular DynamicsProtein DynamicsProtein Folding ThermodynamicsProtein StructureSecondary Structure FormationAmino Acid Sequence EffectsAmino Acid Sequence-structure RelationshipsBackbone Conformational PreferencesFolding PathwaysMolecular Dynamics Of FoldingPeptide FoldingProtein Folding AnalysisProtein Folding Simulations
Accurate reproduction of the mechanism of peptide folding in solution and conformational preferences as a function of amino acid sequence is possible with atomic level dynamics simulations. For example, the simulations correctly predict a left-handed 31-helical fold for the β-heptapeptide 1 (the molecular model is shown in the picture) and a right-handed helical fold for the β-hexapeptide 2, as was confirmed by NMR spectroscopy.