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Published on: December 6, 2012
Recyclization rate of a photocleaved peptide from multiscale simulation
Harald Nieber1, Arnim Hellweg, Nikos L Doltsinis
1Lehrstuhl für Theoretische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Journal of the American Chemical Society
|January 28, 2010
Summary
Phototriggered polypeptide unfolding was simulated using multiscale methods. An intramolecular H-transfer mechanism prevents disulfide bond reformation, potentially resolving scientific debate.
Area of Science:
- Biophysics
- Computational Chemistry
- Molecular Dynamics
Background:
- Polypeptide unfolding is crucial for biological function.
- Disulfide bond reformation rates are poorly understood.
- Phototriggering offers precise control over molecular events.
Purpose of the Study:
- To elucidate the mechanism of phototriggered polypeptide unfolding.
- To investigate the role of disulfide bonds in this process.
- To resolve the controversy surrounding disulfide bond reformation rates.
Main Methods:
- Multiscale simulations combining nonadiabatic ab initio molecular dynamics and classical molecular dynamics.
- A three-stage simulation approach was employed.
- Analysis of intramolecular hydrogen (H)-transfer mechanisms.
Main Results:
- Detailed insight into the phototriggered unfolding pathway.
- Observation of an intramolecular H-transfer mechanism.
- This mechanism saturates disulfide (S-S) radicals, preventing recyclization.
Conclusions:
- The observed H-transfer mechanism acts as a chemical quenching process.
- This mechanism provides a potential explanation for the S-S reformation controversy.
- The findings offer unprecedented understanding of phototriggered molecular events.
