Angewandte Chemie International Edition · 1999 · 1.9K citations · 0 references
EngineeringNmr SpectroscopyPeptide EngineeringMolecular BiologyMolecular DynamicsProtein FoldingPeptide FoldingMolecular SimulationComputational BiochemistryBiophysicsBiochemistryConformational StudyProtein ModelingMolecular ModelingStructural BiologyPeptide LibraryConformational PreferencesMedicineComputational Biophysics
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.