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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8240043
- author
- Bille, Anna
LU
; Linse, Björn
; Mohanty, Sandipan
and Irbäck, Anders
LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Physics
- volume
- 143
- issue
- 17
- article number
- 175102
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- pmid:26547182
- wos:000364585200035
- scopus:84946782609
- pmid:26547182
- 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
- 2016-04-01 10:54:50
- date last changed
- 2023-01-02 17:00:54
@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.}},
author = {{Bille, Anna and Linse, Björn and Mohanty, Sandipan and Irbäck, Anders}},
issn = {{0021-9606}},
language = {{eng}},
number = {{17}},
publisher = {{American Institute of Physics (AIP)}},
series = {{Journal of Chemical Physics}},
title = {{Equilibrium simulation of trp-cage in the presence of protein crowders.}},
url = {{https://lup.lub.lu.se/search/files/2230175/8309705.pdf}},
doi = {{10.1063/1.4934997}},
volume = {{143}},
year = {{2015}},
}