Constrained versus unconstrained folding free-energy landscapes

Autor(en)

Ivan Coluzza

Abstrakt

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(en)

Computergestützte Physik und Physik der Weichen Materie

Journal

Molecular Physics: an international journal in the field of chemical physics

Band

113

Seiten

2905-2912

Anzahl der Seiten

8

ISSN

0026-8976

DOI

https://doi.org/10.1080/00268976.2015.1043031

Publikationsdatum

09-2015

Peer-reviewed

Ja

ÖFOS 2012

106006 Biophysik, 103023 Polymerphysik, 103029 Statistische Physik, 103018 Materialphysik

Schlagwörter

ASJC Scopus Sachgebiete

Condensed Matter Physics, Molecular Biology, Biophysics, Physical and Theoretical Chemistry

Link zum Portal

https://ucrisportal.univie.ac.at/de/publications/74e9ce6c-bf7d-4b37-8a2b-c1c4bd7fbc5c