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dc.contributor.author	McGeoch, Malcolm W
dc.contributor.author	McGeoch, Julie E M
dc.date.accessioned	2010-11-08T18:03:46Z
dc.date.issued	2007
dc.identifier.citation	McGeoch, Julie E. M., and Malcolm W. McGeoch. 2007. Entrapment of water by subunit c of ATP synthase. Journal of the Royal Society Interface 5(20): 311-318.	en_US
dc.identifier.issn	1742-5689	en_US
dc.identifier.uri	http://nrs.harvard.edu/urn-3:HUL.InstRepos:4551484
dc.description.abstract	We consider an ancient protein, and water as a smooth surface, and show that the interaction of the two allows the protein to change its hydrogen bonding to encapsulate the water. This property could have made a three-dimensional microenvironment, 3–4 Gyr ago, for the evolution of subsequent complex water-based chemistry. Proteolipid, subunit c of ATP synthase, when presented with a water surface, changes its hydrogen bonding from an α-helix to β-sheet-like configuration and moves away from its previous association with lipid to interact with water surface molecules. Protein sheets with an intra-sheet backbone spacing of 3.7 Å and inter-sheet spacing of 6.0 Å hydrogen bond into long ribbons or continuous surfaces to completely encapsulate a water droplet. The resulting morphology is a spherical vesicle or a hexagonal crystal of water ice, encased by a skin of subunit c. Electron diffraction shows the crystals to be highly ordered and compressed and the protein skin to resemble β-sheets. The protein skin can retain the entrapped water over a temperature rise from 123 to 223 K at 1×10−4 Pa, whereas free water starts to sublime significantly at 153 K.	en_US
dc.description.sponsorship	Molecular and Cellular Biology	en_US
dc.language.iso	en_US	en_US
dc.publisher	The Royal Society	en_US
dc.relation.isversionof	doi:10.1098/rsif.2007.1146	en_US
dc.relation.hasversion	http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2500151/pdf/	en_US
dash.license	LAA
dc.subject	proteolipid	en_US
dc.subject	encapsulating water	en_US
dc.subject	4 Gyr ago	en_US
dc.title	Entrapment of Water by Subunit C of ATP Synthase	en_US
dc.type	Journal Article	en_US
dc.description.version	Version of Record	en_US
dc.relation.journal	Journal of the Royal Society Interface	en_US
dash.depositing.author	McGeoch, Julie E M
dc.date.available	2010-11-08T18:03:46Z

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  Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University

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