Related Experiment Video
Updated: Aug 13, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
Published on: February 12, 2019
Terminal-group effects on the folding behavior of selected beta-peptides
Peter J Gee1, Wilfred F van Gunsteren
1Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, Zurich, Switzerland.
Abstract:
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.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding Quality Check in the RER
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...

