Projects per year
Abstract
We propose a simple atomic multipole electrostatic model to rapidly evaluate the effects of mutation on enzyme activity and test its performance on wild-type and mutant ketosteroid isomerase. The predictions of our atomic multipole model are similar to those obtained with symmetry-adapted perturbation theory at a fraction of the computational cost. We further show that this approach is relatively insensitive to the precise amino acid side chain conformation in mutants and may thus be useful in computational enzyme (re)design.
Original language | English |
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Pages (from-to) | 945-955 |
Number of pages | 11 |
Journal | Journal of Chemical Theory and Computation |
Volume | 13 |
Issue number | 2 |
Early online date | 19 Jan 2017 |
DOIs | |
Publication status | Published - 14 Feb 2017 |
Structured keywords
- Bristol BioDesign Institute
- BrisSynBio
Keywords
- enzyme catalysis
- ketosteroid isomerase
- cumulative atomic multipole moments
- electrostatic catalysis
Fingerprint
Dive into the research topics of 'Rapid estimation of catalytic efficiency by cumulative atomic multipole moments: application to ketosteroid isomerase mutants'. Together they form a unique fingerprint.Projects
- 11 Finished
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Link account to CHEM RB1768 (EP/M027546/1) - Bristolbridge-Nanospears
11/01/16 → 10/04/16
Project: Research
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Multi-scale enzyme modelling for SynBio: optimizing biocatalysts for selective synthesis of bioactive compounds
1/12/15 → 31/05/21
Project: Research
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CCP-BioSim: Biomolecular Simulation at the Life Sciences Interface
1/07/15 → 30/04/21
Project: Research