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Remarkable patterns of surface water ordering around polarized buckminsterfullerene.

ABSTRACT: Accurate description of water structure affects simulation of protein folding, substrate binding, macromolecular recognition, and complex formation. We study the hydration of buckminsterfullerene, the smallest hydrophobic nanosphere, by molecular dynamics simulations using a state-of-the-art quantum mechanical polarizable force field (QMPFF3), derived from quantum mechanical data at the MP2/aug-cc-pVTZ(-hp) level augmented by CCSD(T). QMPFF3 calculation of the hydrophobic effect is compared to that obtained with empirical force fields. Using a novel and highly sensitive method, we see polarization increases ordered water structure so that the imprint of the hydrophobic surface atoms on the surrounding waters is stronger and extends to long-range. We see less water order for empirical force fields. The greater order seen with QMPFF3 will affect biological processes through a stronger hydrophobic effect.

SUBMITTER: Chopra G

PROVIDER: S-EPMC3167499 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Remarkable patterns of surface water ordering around polarized buckminsterfullerene.

Chopra Gaurav G Levitt Michael M

Proceedings of the National Academy of Sciences of the United States of America 20110815 35

Accurate description of water structure affects simulation of protein folding, substrate binding, macromolecular recognition, and complex formation. We study the hydration of buckminsterfullerene, the smallest hydrophobic nanosphere, by molecular dynamics simulations using a state-of-the-art quantum mechanical polarizable force field (QMPFF3), derived from quantum mechanical data at the MP2/aug-cc-pVTZ(-hp) level augmented by CCSD(T). QMPFF3 calculation of the hydrophobic effect is compared to t ...[more]

PMID: 21844369

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Project description:Hydrophobic matching, lipid sorting, and protein oligomerization are key principles by which lipids and proteins organize in biological membranes. The Aquaporin-0 channel (AQP0), solved by electron crystallography (EC) at cryogenic temperatures, is one of the few protein-lipid complexes of which the structure is available in atomic detail. EC and room-temperature molecular dynamics (MD) of dimyristoylglycerophosphocholine (DMPC) annular lipids around AQP0 show similarities, however, crystal-packing and temperature might affect the protein surface or the lipids distribution. To understand the role of temperature, lipid phase, and protein mobility in the localization and ordering of AQP0-lipids, we used MD simulations of an AQP0-DMPC bilayer system. Simulations were performed at physiological and at DMPC gel-phase temperatures. To decouple the protein and lipid mobility effects, we induced gel-phase in the lipids or restrained the protein. We monitored the lipid ordering effects around the protein. Reducing the system temperature or inducing lipid gel-phase had a marginal effect on the annular lipid localization. However, restraining the protein mobility increased the annular lipid localization around the whole AQP0 surface, resembling EC. The distribution of the inter-phosphate and hydrophobic thicknesses showed that stretching of the DMPC annular layer around AQP0 surface is the mechanism that compensates the hydrophobic mismatch in this system. The distribution of the local area-per-lipid and the acyl-chain order parameters showed particular fluid- and gel-like areas that involved several lipid layers. These areas were in contact with the surfaces of higher and lower protein mobility, respectively. We conclude that the AQP0 surfaces induce specific fluid- and gel-phase prone areas. The presence of these areas might guide the AQP0 lipid sorting interactions with other membrane components, and is compatible with the squared array oligomerization of AQP0 tetramers separated by a layer of annular lipids.

Dataset Information

Remarkable patterns of surface water ordering around polarized buckminsterfullerene.

Publications

Remarkable patterns of surface water ordering around polarized buckminsterfullerene.

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