Data from: Functional regulation of aquaporin dynamics by lipid bilayer composition

With the diversity of lipid-protein interactions, any observed membrane
protein dynamics or functions directly depend on the lipid bilayer
selection. However, the implications of lipid bilayer choice are seldom
considered unless characteristic lipid-protein interactions have been
previously reported. Using molecular dynamics simulation, we characterize
the effects of membrane embedding on plant aquaporin SoPIP2;1, which has
no reported high-affinity lipid interactions. The regulatory impacts of a
realistic lipid bilayer, and nine different homogeneous bilayers, on
varying SoPIP2;1 dynamics were examined. We demonstrate that
SoPIP2;1's structure, thermodynamics, kinetics, and water transport
are altered as a function of each membrane construct's ensemble
properties. Notably, the realistic bilayer provides stabilization of
non-functional SoPIP2;1 metastable states. Hydrophobic mismatch and lipid
order parameter calculations further explain how lipid ensemble proprties
manipulate SoPIP2;1 behavior. Our results illustrate the importance of
careful bilayer selection when studying membrane proteins. To this end, we
advise cautionary measures when performing membrane protein moelcular
dynamics simulations.