
Anders Irbäck
Professor

Peptide folding in the presence of interacting protein crowders
Author
Summary, in English
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.
Department/s
- Computational Biology and Biological Physics - Undergoing reorganization
- eSSENCE: The e-Science Collaboration
Publishing year
2016-05-07
Language
English
Publication/Series
Journal of Chemical Physics
Volume
144
Issue
17
Document type
Journal article
Publisher
American Institute of Physics (AIP)
Topic
- Other Physics Topics
- Biophysics
Status
Published
ISBN/ISSN/Other
- ISSN: 0021-9606