Ontology highlight
ABSTRACT:
SUBMITTER: Paulino J
PROVIDER: S-EPMC6428927 | biostudies-literature | 2019 Mar
REPOSITORIES: biostudies-literature
Biophysical journal 20190210 6
Protein dynamics in crowded environments is important for understanding protein functions in vivo and is especially relevant for membrane proteins because of the roles of protein-protein interactions in membrane protein functions and their regulation. Here, using solid-state NMR spectroscopy in combination with coarse-grained molecular dynamics simulations, we report that the rotational correlation time for the transmembrane domain of the influenza A M2 proton channel in lipid bilayers increases ...[more]