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 |
|---|---|
| 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 |
|---|---|
| Directorate for Biological Sciences | 1021374 |
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