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Effects of end-group termination on salting-out constants for triglycine

Hladílková, Jana LU ; Heyda, Jan ; Rembert, Kelvin B. ; Okur, Halil I. ; Kurra, Yadagiri ; Liu, Wenshe R. ; Hilty, Christian ; Cremer, Paul S. and Jungwirth, Pavel (2013) In Journal of Physical Chemistry Letters 4(23). p.4069-4073
Abstract

Salting-out constants for triglycine were calculated for a series of Hofmeister salts using molecular dynamics simulations. Three variants of the peptide were considered with both termini capped, just the N-terminus capped, and without capping. The simulations were supported by NMR and FTIR measurements. The data provide strong evidence that previous experimental values of salting-out constants assigned to the fully capped peptide (as previously assumed) should have been assigned to the half-capped peptide instead. Therefore, these values cannot be used to directly establish Hofmeister ordering of ions at the peptide backbone because they are strongly influenced by interactions of the ions with the negatively charged C terminus.

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author
; ; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Hofmeister series, ions, molecular dynamics, NMR, triglycine
in
Journal of Physical Chemistry Letters
volume
4
issue
23
pages
5 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:84890417895
ISSN
1948-7185
DOI
10.1021/jz4022238
language
English
LU publication?
no
id
9423776f-2c4d-4ae6-a22e-b66de509b98d
date added to LUP
2025-07-18 11:22:36
date last changed
2025-08-28 10:56:11
@article{9423776f-2c4d-4ae6-a22e-b66de509b98d,
  abstract     = {{<p>Salting-out constants for triglycine were calculated for a series of Hofmeister salts using molecular dynamics simulations. Three variants of the peptide were considered with both termini capped, just the N-terminus capped, and without capping. The simulations were supported by NMR and FTIR measurements. The data provide strong evidence that previous experimental values of salting-out constants assigned to the fully capped peptide (as previously assumed) should have been assigned to the half-capped peptide instead. Therefore, these values cannot be used to directly establish Hofmeister ordering of ions at the peptide backbone because they are strongly influenced by interactions of the ions with the negatively charged C terminus.</p>}},
  author       = {{Hladílková, Jana and Heyda, Jan and Rembert, Kelvin B. and Okur, Halil I. and Kurra, Yadagiri and Liu, Wenshe R. and Hilty, Christian and Cremer, Paul S. and Jungwirth, Pavel}},
  issn         = {{1948-7185}},
  keywords     = {{Hofmeister series; ions; molecular dynamics; NMR; triglycine}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{23}},
  pages        = {{4069--4073}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Physical Chemistry Letters}},
  title        = {{Effects of end-group termination on salting-out constants for triglycine}},
  url          = {{http://dx.doi.org/10.1021/jz4022238}},
  doi          = {{10.1021/jz4022238}},
  volume       = {{4}},
  year         = {{2013}},
}