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Title: Influence of Hofmeister ions on the structure of proline-based peptide models: A combined experimental and molecular modeling study

Here, the influence of three sodium salts, covering a wide range of the Hofmeister series, on the conformation of three proline-based peptide models in aqueous solution is examined using a combination of nuclear magnetic resonance spectroscopy and molecular dynamics simulations. The anions preferentially interact with the cis conformers of the peptide models, which is rationalized by the respective electrostatic potential surfaces. These preferred interactions have a strong impact on the thermodynamics of the cis/trans equilibria, leading to a higher population of the cis conformers. In distinct cases, these equilibria are nearly independent of temperature, showing that the salts are also able to stabilize the conformers over wide temperature ranges.
Authors:
 [1] ;  [1] ;  [2] ; ORCiD logo [2] ; ORCiD logo [1]
  1. Univ. of Cologne, Cologne (Germany)
  2. Univ. of Notre Dame, Notre Dame, IN (United States)
Publication Date:
Grant/Contract Number:
AC02-06CH11357
Type:
Published Article
Journal Name:
Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry
Additional Journal Information:
Journal Volume: 121; Journal Issue: 9; Journal ID: ISSN 1520-6106
Publisher:
American Chemical Society
Research Org:
Univ. of Notre Dame, Notre Dame, IN (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
OSTI Identifier:
1344583
Alternate Identifier(s):
OSTI ID: 1346406