Mutational Basin-Hopping: Combined Structure and Sequence Optimization for Biomolecules.
J Phys Chem Lett
American Chemical Society (ACS)
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Röder, K., & Wales, D. J. (2018). Mutational Basin-Hopping: Combined Structure and Sequence Optimization for Biomolecules.. J Phys Chem Lett, 9 (21), 6169-6173. https://doi.org/10.1021/acs.jpclett.8b02839
The study of energy landscapes has led to a good understanding of how and why proteins and nucleic acids adopt their native structure. Through evolution, sequences have adapted until they exhibit a strongly funneled energy landscape, stabilizing the native fold. Design of artificial biomolecules faces the challenge of creating similar stable, minimally frustrated, and functional sequences. Here we present a biminimization approach, mutational basin-hopping, in which we simultaneously use global optimization to optimize the energy and a target function describing a desired property of the system. This optimization of structure and sequence is a generalized basin-hopping method and produces an efficient design process, which can target properties such as binding affinity or solubility.
Oxytocin, Vasopressins, Neurophysins, Proteins, Ligands, Protein Folding, Mutation, Algorithms, Thermodynamics, Models, Chemical, Models, Molecular
Engineering and Physical Sciences Research Council (EP/N035003/1)
External DOI: https://doi.org/10.1021/acs.jpclett.8b02839
This record's URL: https://www.repository.cam.ac.uk/handle/1810/286342