Publisher: American Chemical Society (ACS)

Issue: 2

License: http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html

Publication date(s): 2017/02/14 (print) 2017/02/02 (online)

Pages: 945-955

Volume: 13 Issue: 2

Journal: Journal of Chemical Theory and Computation

Link: http://pubs.acs.org/doi/pdf/10.1021/acs.jctc.6b01131

URL: http://dx.doi.org/10.1021/acs.jctc.6b01131

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.