@article{e8f0a32f112143cfbc4fce951d0b7020,
title = "Atomistic characterization of collective protein-water-membrane dynamics",
abstract = "Correlated vibrational motion on the sub-picosecond timescale and associated collective dynamics in a protein-membrane environment are characterized using molecular dynamics simulations. We specifically analyze correlated motion of a membrane-associated protein and a lipid bilayer for distinct separation distances. Correlated vibrations persist up to distances of 25 {\AA} between both biomolecular surfaces. These correlations are mediated by separating layers of water molecules, whose collective properties are altered by the simultaneous presence of protein and lipid bilayer interfaces.",
author = "Christopher P{\"a}slack and Schafer, {Lars V.} and Matthias Heyden",
note = "Funding Information: Here, we characterized correlated low-frequency vibrations between the membrane-associated protein annexin B12 (Anx) and a lipid bilayer consisting of a 7 : 3 mixture of DOPC and DOPS lipids (Fig. 1). We further analyzed correlated vibrations of protein and lipid atoms with water separating both biomolecular surfaces. Atomic vibrations were sampled in all-atom molecular dynamics (MD) simulations and their correlations were analyzed for membrane-bound and unbound states. This analysis revealed the persistence of correlated vibrations between atoms of the Anx protein and membrane lipids up to 25 {\AA} separation distances, which are mediated by the separating shell of hydration water. This finding is supported by the observation of simultaneous modifications of collective protein–water and lipid–water dynamics, which describe the propagation of collective modes from the protein and lipid bilayer surfaces into water layers separating both. A complementary analysis in the time-domain provides an estimate for the exchange of information with respect to the average thermal energy via the collective modes described here. Publisher Copyright: {\textcopyright} the Owner Societies.",
year = "2019",
doi = "10.1039/c9cp00725c",
language = "English (US)",
volume = "21",
pages = "15958--15965",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
publisher = "Royal Society of Chemistry",
number = "29",
}