@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{\textendash}water and lipid{\textendash}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",
}