Urea–Water Solvation Forces on Prion Structures
Solvation forces are crucial determinants in the equilibrium between the folded and unfolded state of proteins. Particularly interesting are the solvent forces of denaturing solvent mixtures on folded and misfolded states of proteins involved in neurodegeneration. The C-terminal globular domain of t...
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American Chemical Society
2012
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3466777/ |
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pubmed-34667772012-10-10 Urea–Water Solvation Forces on Prion Structures Kleinjung, Jens Fraternali, Franca Solvation forces are crucial determinants in the equilibrium between the folded and unfolded state of proteins. Particularly interesting are the solvent forces of denaturing solvent mixtures on folded and misfolded states of proteins involved in neurodegeneration. The C-terminal globular domain of the ovine prion protein (1UW3) and its analogue H2H3 in the α-rich and β-rich conformation were used as model structures to study the solvation forces in 4 M aqueous urea using molecular dynamics. The model structures display very different secondary structures and solvent exposures. Most protein atoms favor interactions with urea over interactions with water. The force difference between protein–urea and protein–water interactions correlates with hydrophobicity; i.e., urea interacts preferentially with hydrophobic atoms, in agreement with results from solvent transfer experiments. Solvent Shannon entropy maps illustrate the mobility gradient of the urea–water mixture from the first solvation shell to the bulk. Single urea molecules replace water in the first solvation shell preferably at locations of relatively high solvent entropy. American Chemical Society 2012-08-14 2012-10-09 /pmc/articles/PMC3466777/ /pubmed/23066353 http://dx.doi.org/10.1021/ct300264w Text en Copyright © 2012 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Kleinjung, Jens Fraternali, Franca |
| spellingShingle |
Kleinjung, Jens Fraternali, Franca Urea–Water Solvation Forces on Prion Structures |
| author_facet |
Kleinjung, Jens Fraternali, Franca |
| author_sort |
Kleinjung, Jens |
| title |
Urea–Water Solvation
Forces on Prion Structures |
| title_short |
Urea–Water Solvation
Forces on Prion Structures |
| title_full |
Urea–Water Solvation
Forces on Prion Structures |
| title_fullStr |
Urea–Water Solvation
Forces on Prion Structures |
| title_full_unstemmed |
Urea–Water Solvation
Forces on Prion Structures |
| title_sort |
urea–water solvation
forces on prion structures |
| description |
Solvation forces are crucial determinants in the equilibrium
between
the folded and unfolded state of proteins. Particularly interesting
are the solvent forces of denaturing solvent mixtures on folded and
misfolded states of proteins involved in neurodegeneration. The C-terminal
globular domain of the ovine prion protein (1UW3) and its analogue
H2H3 in the α-rich and β-rich conformation were used as
model structures to study the solvation forces in 4 M aqueous urea
using molecular dynamics. The model structures display very different
secondary structures and solvent exposures. Most protein atoms favor
interactions with urea over interactions with water. The force difference
between protein–urea and protein–water interactions
correlates with hydrophobicity; i.e., urea interacts preferentially
with hydrophobic atoms, in agreement with results from solvent transfer
experiments. Solvent Shannon entropy maps illustrate the mobility
gradient of the urea–water mixture from the first solvation
shell to the bulk. Single urea molecules replace water in the first
solvation shell preferably at locations of relatively high solvent
entropy. |
| publisher |
American Chemical Society |
| publishDate |
2012 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3466777/ |
| _version_ |
1611914512581001216 |