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Kinetics of breaking a salt-bridge critical in protein unfolding

Chemical Physics Letters, ISSN: 0009-2614, Vol: 385, Issue: 5, Page: 337-340
2004
  • 15
    Citations
  • 0
    Usage
  • 30
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    15
    • Citation Indexes
      15
  • Captures
    30

Article Description

The rate of breaking an Arg–Glu salt bridge on the surface of a globular protein (Staphylococcal nuclease) is determined by using molecular dynamics simulations to derive the free energy activation barrier to dissociation and the pre-exponential rate factor for that reaction. The dissociation barrier obtained is 7 kcal/mol. The pre-exponential factor is derived using a novel method in which simulations are performed for the same system with the salt bridge weakened such that the rate can be observed directly. Combining the prefactor thus obtained (5×10 11 s −1 ) with the above dissociation barrier height yields an estimated lifetime of the salt-bridge of 200 ns, suggesting that surface salt-bridges can cause significant kinetic barriers to protein folding or unfolding.

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