Abstract
Monte Carlo (MC) simulations with a fixed protein backbone but mobile sidechains are common for acid/base constants and protein design. To characterize the fluctuations in these models, estimating the Fröhlich-Kirkwood dielectric constant can give physical insight and allow comparison both with models that are more rigorous (fully flexible) and ones that are simpler (Poisson-Boltmann without any explicit protein flexibility). MC simulations of two small proteins yield protein dielectric constants of 12 and 14, about 70% of the result from MD (16 and 22). Thus, the consistency between the fully explicit MD and partly explicit MC is only fair.
| Original language | English |
|---|---|
| Pages (from-to) | 4603-4608 |
| Number of pages | 6 |
| Journal | Journal of Chemical Theory and Computation |
| Volume | 9 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 8 Oct 2013 |
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