Abstract
Salt-bridges ubiquitously form between oppositely charged moieties in proteins. Here we quantify changes in population of salt-bridged β-hairpin peptides due to added salt, and determine the thermodynamic driving forces and cooperativity of salt-bridge formation under these conditions. We find only a fraction of salt-bridged folded conformations at physiologically relevant salt concentrations.
| Original language | English |
|---|---|
| Pages (from-to) | 8193-8196 |
| Number of pages | 4 |
| Journal | Chemical Communications |
| Volume | 50 |
| Issue number | 60 |
| DOIs | |
| State | Published - 1 Jul 2014 |