Mutational Basin-Hopping: Combined Structure and Sequence Optimization for Biomolecules.
The journal of physical chemistry letters
American Chemical Society (ACS)
MetadataShow full item record
Roeder, K., & Wales, D. (2018). Mutational Basin-Hopping: Combined Structure and Sequence Optimization for Biomolecules.. The journal of physical chemistry letters, 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 funnelled energy landscape, stabilising the native fold. Design of artificial biomolecules faces the challenge of creating similar stable, minimally frustrated and functional sequences. Here we present a biminimisation approach, mutational basin-hopping, in which we simultaneously use global optimisation to optimise the energy and a target function describing a desired property of the system. This optimisation of structure and sequence is a generalised 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
External DOI: https://doi.org/10.1021/acs.jpclett.8b02839
This record's URL: https://www.repository.cam.ac.uk/handle/1810/286342