Evolved Minimal Frustration in Multifunctional Biomolecules.
J Phys Chem B
American Chemical Society (ACS)
MetadataShow full item record
Röder, K., & Wales, D. J. (2018). Evolved Minimal Frustration in Multifunctional Biomolecules.. J Phys Chem B, 122 (49), 10989-10995. https://doi.org/10.1021/acs.jpcb.8b03632
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.
Mutation, Protein Engineering, Protein Folding, Proteins, Thermodynamics
Engineering and Physical Sciences Research Council (EP/N035003/1)
External DOI: https://doi.org/10.1021/acs.jpcb.8b03632
This record's URL: https://www.repository.cam.ac.uk/handle/1810/279738
Attribution 4.0 International (CC BY 4.0)
Licence URL: https://creativecommons.org/licenses/by/4.0/
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