Juraszek, J;
Saladino, G;
van Erp, TS;
Gervasio, FL;
(2013)
Efficient numerical reconstruction of protein folding kinetics with partial path sampling and pathlike variables.
Phys Rev Lett
, 110
(10)
, Article 108106. 10.1103/PhysRevLett.110.108106.
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Abstract
Numerically predicting rate constants of protein folding and other relevant biological events is still a significant challenge. We show that the combination of partial path transition interface sampling with the optimal interfaces and free-energy profiles provided by path collective variables makes the rate calculation for practical biological applications feasible and efficient. This methodology can reproduce the experimental rate constant of Trp-cage miniprotein folding with the same level of accuracy as transition path sampling at a fraction of the cost.
| Type: | Article |
|---|---|
| Title: | Efficient numerical reconstruction of protein folding kinetics with partial path sampling and pathlike variables. |
| Location: | United States |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1103/PhysRevLett.110.108106 |
| Publisher version: | http://dx.doi.org/10.1103/PhysRevLett.110.108106 |
| Language: | English |
| Additional information: | © 2013 American Physical Society |
| Keywords: | Hydrophobic and Hydrophilic Interactions, Kinetics, Models, Chemical, Models, Molecular, Peptides, Protein Folding, Protein Structure, Secondary, Thermodynamics |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > UCL BEAMS UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Chemistry |
| URI: | https://discovery.ucl.ac.uk/id/eprint/1389039 |
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