Entrapment of Water by Subunit C of ATP Synthase

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Entrapment of Water by Subunit C of ATP Synthase

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Title: Entrapment of Water by Subunit C of ATP Synthase
Author: McGeoch, Malcolm W; McGeoch, Julie E M

Note: Order does not necessarily reflect citation order of authors.

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.
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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.
Published Version: doi:10.1098/rsif.2007.1146
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2500151/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4551484

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  • FAS Scholarly Articles [7289]
    Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University
 
 

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