Equilibrium simulation of trp-cage in the presence of protein crowders.
(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
- 2024-04-22 00:47:46
@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}}, }