Peptide folding in the presence of interacting protein crowders
Bille, Anna LU ; Mohanty, Sandipan and Irbäck, Anders LU
(2016)
In Journal of Chemical Physics
144(17).
- Abstract
Using Monte Carlo methods, we explore and compare the effects of two protein crowders, BPTI and GB1, on the folding thermodynamics of two peptides, the compact helical trp-cage and the β-hairpin-forming GB1m3. The thermally highly stable crowder proteins are modeled using a fixed backbone and rotatable side-chains, whereas the peptides are free to fold and unfold. In the simulations, the crowder proteins tend to distort the trp-cage fold, while having a stabilizing effect on GB1m3. The extent of the effects on a given peptide depends on the crowder type. Due to a sticky patch on its surface, BPTI causes larger changes than GB1 in the melting properties of the peptides. The observed effects on the peptides stem largely from attractive... (More)
Using Monte Carlo methods, we explore and compare the effects of two protein crowders, BPTI and GB1, on the folding thermodynamics of two peptides, the compact helical trp-cage and the β-hairpin-forming GB1m3. The thermally highly stable crowder proteins are modeled using a fixed backbone and rotatable side-chains, whereas the peptides are free to fold and unfold. In the simulations, the crowder proteins tend to distort the trp-cage fold, while having a stabilizing effect on GB1m3. The extent of the effects on a given peptide depends on the crowder type. Due to a sticky patch on its surface, BPTI causes larger changes than GB1 in the melting properties of the peptides. The observed effects on the peptides stem largely from attractive and specific interactions with the crowder surfaces, and differ from those seen in reference simulations with purely steric crowder particles.
(Less)
- author
- Bille, Anna
LU
; Mohanty, Sandipan
and Irbäck, Anders
LU
- organization
- publishing date
- 2016-05-07
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Physics
- volume
- 144
- issue
- 17
- article number
- 175105
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- pmid:27155657
- scopus:84973640757
- wos:000377711300043
- ISSN
- 0021-9606
- DOI
- 10.1063/1.4948462
- language
- English
- LU publication?
- yes
- id
- bcdd0877-27aa-4226-b23a-4ca76eac6201
- date added to LUP
- 2016-08-16 18:15:53
- date last changed
- 2024-04-19 07:04:21
@article{bcdd0877-27aa-4226-b23a-4ca76eac6201,
abstract = {{<p>Using Monte Carlo methods, we explore and compare the effects of two protein crowders, BPTI and GB1, on the folding thermodynamics of two peptides, the compact helical trp-cage and the β-hairpin-forming GB1m3. The thermally highly stable crowder proteins are modeled using a fixed backbone and rotatable side-chains, whereas the peptides are free to fold and unfold. In the simulations, the crowder proteins tend to distort the trp-cage fold, while having a stabilizing effect on GB1m3. The extent of the effects on a given peptide depends on the crowder type. Due to a sticky patch on its surface, BPTI causes larger changes than GB1 in the melting properties of the peptides. The observed effects on the peptides stem largely from attractive and specific interactions with the crowder surfaces, and differ from those seen in reference simulations with purely steric crowder particles.</p>}},
author = {{Bille, Anna and Mohanty, Sandipan and Irbäck, Anders}},
issn = {{0021-9606}},
language = {{eng}},
month = {{05}},
number = {{17}},
publisher = {{American Institute of Physics (AIP)}},
series = {{Journal of Chemical Physics}},
title = {{Peptide folding in the presence of interacting protein crowders}},
url = {{http://dx.doi.org/10.1063/1.4948462}},
doi = {{10.1063/1.4948462}},
volume = {{144}},
year = {{2016}},
}