Analysis of fast boundary-integral approximations for modeling electrostatic contributions of molecular binding.

ABSTRACT: We analyze and suggest improvements to a recently developed approximate continuum-electrostatic model for proteins. The model, called BIBEE/I (boundary-integral based electrostatics estimation with interpolation), was able to estimate electrostatic solvation free energies to within a mean unsigned error of 4% on a test set of more than 600 proteins-a significant improvement over previous BIBEE models. In this work, we tested the BIBEE/I model for its capability to predict residue-by-residue interactions in protein-protein binding, using the widely studied model system of trypsin and bovine pancreatic trypsin inhibitor (BPTI). Finding that the BIBEE/I model performs surprisingly less well in this task than simpler BIBEE models, we seek to explain this behavior in terms of the models' differ

SUBMITTER: Kreienkamp AB 

PROVIDER: S-EPMC3897805 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature