Entrapment of Water by Subunit C of ATP Synthase
| 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. |
| Full Text & Related Files: |
2500151.pdf (650.5Kb; PDF) 
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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/ |
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| Citable link to this page: | http://nrs.harvard.edu/urn-3:HUL.InstRepos:4551484 |
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