Constrained versus unconstrained folding free-energy landscapes
- Author(s)
- Ivan Coluzza
- Abstract
Protein folding can be described as a downhill process that brings the configuration of a chain of amino acids down to the bottom of a smooth free-energy funnel. Here, we use a recently developed coarse-grained protein model to assess the importance of frustration in the folding free-energy landscape. We compare the landscapes of natural proteins, computationally designed sequences, and structure-based potentials that force the contacts between the amino acids to adopt the native structure. Our results show that the structure-based potentials give a poor representation of the folding free-energy landscape, and that frustration is not just a perturbation over an otherwise perfect downhill folding.
- Organisation(s)
- Computational and Soft Matter Physics
- Journal
- Molecular Physics: an international journal in the field of chemical physics
- Volume
- 113
- Pages
- 2905-2912
- No. of pages
- 8
- ISSN
- 0026-8976
- DOI
- https://doi.org/10.1080/00268976.2015.1043031
- Publication date
- 09-2015
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 106006 Biophysics, 103023 Polymer physics, 103029 Statistical physics, 103018 Materials physics
- Keywords
- ASJC Scopus subject areas
- Condensed Matter Physics, Molecular Biology, Biophysics, Physical and Theoretical Chemistry
- Portal url
- https://ucrisportal.univie.ac.at/en/publications/74e9ce6c-bf7d-4b37-8a2b-c1c4bd7fbc5c