Abstract
Replacement of the hydroxyl group of a hydrophilic sidechain by an H atom in the proton wire of GFP induces formation of a water-chain proton wire. Surprisingly, this "non-native" water chain functions as a proton wire with response times within 10 ps of the wild type protein. This remarkable rate retention is understood as a natural consequence of the well-known Grotthuss mechanism of proton transfer in water.
Original language | English |
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Pages (from-to) | 23089-23095 |
Number of pages | 7 |
Journal | Physical Chemistry Chemical Physics |
Volume | 18 |
Issue number | 33 |
DOIs | |
State | Published - 2016 |
Externally published | Yes |
Bibliographical note
Publisher Copyright:© 2016 the Owner Societies.
Funding
Funders | Funder number |
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Directorate for Biological Sciences | 1021374 |