Capturing Choline-Aromatics Cation-π Interactions in the MARTINI Force Field.

ABSTRACT: Cation-π interactions play an important role in biomolecular recognition, including interactions between membrane phosphatidylcholine lipids and aromatic amino acids of peripheral proteins. While molecular mechanics coarse grain (CG) force fields are particularly well suited to simulate membrane proteins in general, they are not parameterized to explicitly reproduce cation-π interactions. We here propose a modification of the polarizable MARTINI coarse grain (CG) model enabling it to model membrane binding events of peripheral proteins whose aromatic amino acid interactions with choline headgroups are crucial for their membrane binding. For this purpose, we first collected and curated a dataset of eight peripheral proteins from different families. We find that the MARTINI CG model expected

SUBMITTER: Khan HM 

PROVIDER: S-EPMC7175457 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature