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Equilibrium simulation of trp-cage in the presence of protein crowders.

Bille, Anna LU ; Linse, Björn; Mohanty, Sandipan and Irbäck, Anders LU (2015) In Journal of Chemical Physics 143(17).
Abstract
While steric crowders tend to stabilize globular proteins, it has been found that protein crowders can have an either stabilizing or destabilizing effect, where a destabilization may arise from nonspecific attractive interactions between the test protein and the crowders. Here, we use Monte Carlo replica-exchange methods to explore the equilibrium behavior of the miniprotein trp-cage in the presence of protein crowders. Our results suggest that the surrounding crowders prevent trp-cage from adopting its global native fold, while giving rise to a stabilization of its main secondary-structure element, an α-helix. With the crowding agent used (bovine pancreatic trypsin inhibitor), the trp-cage-crowder interactions are found to be specific,... (More)
While steric crowders tend to stabilize globular proteins, it has been found that protein crowders can have an either stabilizing or destabilizing effect, where a destabilization may arise from nonspecific attractive interactions between the test protein and the crowders. Here, we use Monte Carlo replica-exchange methods to explore the equilibrium behavior of the miniprotein trp-cage in the presence of protein crowders. Our results suggest that the surrounding crowders prevent trp-cage from adopting its global native fold, while giving rise to a stabilization of its main secondary-structure element, an α-helix. With the crowding agent used (bovine pancreatic trypsin inhibitor), the trp-cage-crowder interactions are found to be specific, involving a few key residues, most of which are prolines. The effects of these crowders are contrasted with those of hard-sphere crowders. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Chemical Physics
volume
143
issue
17
publisher
American Institute of Physics
external identifiers
  • pmid:26547182
  • wos:000364585200035
  • scopus:84946782609
ISSN
0021-9606
DOI
10.1063/1.4934997
language
English
LU publication?
yes
id
ddc48732-2cc5-479d-8fcb-5766084dfc8c (old id 8240043)
date added to LUP
2015-12-08 23:10:55
date last changed
2017-11-05 03:20:56
@article{ddc48732-2cc5-479d-8fcb-5766084dfc8c,
  abstract     = {While steric crowders tend to stabilize globular proteins, it has been found that protein crowders can have an either stabilizing or destabilizing effect, where a destabilization may arise from nonspecific attractive interactions between the test protein and the crowders. Here, we use Monte Carlo replica-exchange methods to explore the equilibrium behavior of the miniprotein trp-cage in the presence of protein crowders. Our results suggest that the surrounding crowders prevent trp-cage from adopting its global native fold, while giving rise to a stabilization of its main secondary-structure element, an α-helix. With the crowding agent used (bovine pancreatic trypsin inhibitor), the trp-cage-crowder interactions are found to be specific, involving a few key residues, most of which are prolines. The effects of these crowders are contrasted with those of hard-sphere crowders.},
  articleno    = {175102},
  author       = {Bille, Anna and Linse, Björn and Mohanty, Sandipan and Irbäck, Anders},
  issn         = {0021-9606},
  language     = {eng},
  number       = {17},
  publisher    = {American Institute of Physics},
  series       = {Journal of Chemical Physics},
  title        = {Equilibrium simulation of trp-cage in the presence of protein crowders.},
  url          = {http://dx.doi.org/10.1063/1.4934997},
  volume       = {143},
  year         = {2015},
}