Terminal-group effects on the folding behavior of selected beta-peptides.
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.
Gee
Peter J
PJ
Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, Zurich, Switzerland.
van Gunsteren
Wilfred F
WF
D003198:Computer Simulation; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009842:Oligopeptides; D010452:Peptide Biosynthesis; D010446:Peptide Fragments; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D040901:Proteomics / Q000379:methods*; D012984:Software; D013053:Spectrophotometry / Q000379:methods*; D013816:Thermodynamics; D013997:Time Factors
D009842:Oligopeptides; D010446:Peptide Fragments; D010455:Peptides