Evolved Minimal Frustration in Multifunctional Biomolecules.
Published version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Röder, Konstantin https://orcid.org/0000-0003-2021-9504
Wales, David J https://orcid.org/0000-0002-3555-6645
Abstract
Protein folding is often viewed in terms of a funneled potential or free energy landscape. A variety of experiments now indicate the existence of multifunnel landscapes, associated with multifunctional biomolecules. Here, we present evidence that these systems have evolved to exhibit the minimal number of funnels required to fulfill their cellular functions, suggesting an extension to the principle of minimum frustration. We find that minimal disruptive mutations result in additional funnels, and the associated structural ensembles become more diverse. The same trends are observed in an atomic cluster. These observations suggest guidelines for rational design of engineered multifunctional biomolecules.
Description
Keywords
Mutation, Protein Engineering, Protein Folding, Proteins, Thermodynamics
Journal Title
J Phys Chem B
Conference Name
Journal ISSN
1520-6106
1520-5207
1520-5207
Volume Title
122
Publisher
American Chemical Society (ACS)
Publisher DOI
Sponsorship
EPSRC (1652488)
Engineering and Physical Sciences Research Council (EP/N035003/1)
Engineering and Physical Sciences Research Council (EP/N035003/1)