Kinetics of breaking a salt-bridge critical in protein unfolding
Chemical Physics Letters, ISSN: 0009-2614, Vol: 385, Issue: 5, Page: 337-340
2004
- 15Citations
- 30Captures
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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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0009261403021717; http://dx.doi.org/10.1016/j.cplett.2003.12.038; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=1242293740&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/S0009261403021717; https://api.elsevier.com/content/article/PII:S0009261403021717?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:S0009261403021717?httpAccept=text/plain; https://dx.doi.org/10.1016/j.cplett.2003.12.038
Elsevier BV
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