Ontology highlight
ABSTRACT:
SUBMITTER: Naughton FB
PROVIDER: S-EPMC5593124 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Naughton Fiona B FB Kalli Antreas C AC Sansom Mark S P MS
The journal of physical chemistry letters 20160317 7
Understanding the energetics of peripheral protein-membrane interactions is important to many areas of biophysical chemistry and cell biology. Estimating free-energy landscapes by molecular dynamics (MD) simulation is challenging for such systems, especially when membrane recognition involves complex lipids, e.g., phosphatidylinositol phosphates (PIPs). We combined coarse-grained MD simulations with umbrella sampling to quantify the binding of the well-explored GRP1 pleckstrin homology (PH) doma ...[more]