Gee PJ van Gunsteren WF 2006 It has been suggested that the stability of a beta-peptide helical fold is affected by the interplay between the electrical charge of terminal groups and the dipole due to the helical conformation, the so-called charge-dipole stabilization; the numerical simulations presented herein test that suggestion. The motions of two beta-peptide oligomers, each of which has been shown by NMR spectroscopy to fold into a different helical conformation, have been simulated. The simulated motions bear out empirical observations as to the effect of chemical protection of terminal groups on the stability of beta-peptide helical folds and they support the hypothesis of charge-dipole stabilization. https://sonar.ch/global/documents/47241 eng info:eu-repo/semantics/altIdentifier/doi/10.1002/prot.20839 info:eu-repo/semantics/altIdentifier/pmid/16435370 Proteins. - 2006 Computer Simulation Hydrogen Bonding Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Models, Chemical Models, Molecular Molecular Conformation Molecular Sequence Data Oligopeptides Peptide Biosynthesis Peptide Fragments Peptides Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Proteomics Software Spectrophotometry Thermodynamics Time Factors Terminal-group effects on the folding behavior of selected beta-peptides. http://purl.org/coar/resource_type/c_6501