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Terminal-group effects on the folding behavior of selected beta-peptides.
Journal article

Terminal-group effects on the folding behavior of selected beta-peptides.

  • Gee PJ Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, Zurich, Switzerland.
  • van Gunsteren WF
  • 2006-01-26
Published in:
  • 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
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/47241
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