Reaction coordinates of biomolecular isomerization
- Author(s)
- Peter G Bolhuis, Christoph Dellago, David Chandler
- Abstract
Transition path sampling has been applied to the molecular dynamics of the alanine dipeptide in vacuum and in aqueous solution. The analysis shows that more degrees of freedom than the traditional dihedral angles, f and ?, are necessary to describe the reaction coordinates for isomerization of this molecule. In vacuum, an additional dihedral angle is identified as significant. In solution, solvent variables are shown to play a significant role, and this role appears to be more specific than can be captured by friction models. Implications for larger molecules are discussed.
- Organisation(s)
- Computational and Soft Matter Physics
- External organisation(s)
- University of Amsterdam (UvA), University of California, Berkeley
- Journal
- Proceedings of the National Academy of Sciences of the United States of America (PNAS)
- Volume
- 97
- Pages
- 5877-5882
- No. of pages
- 6
- ISSN
- 0027-8424
- DOI
- https://doi.org/10.1073/pnas.100127697
- Publication date
- 2000
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 1030 Physics, Astronomy
- Portal url
- https://ucrisportal.univie.ac.at/en/publications/reaction-coordinates-of-biomolecular-isomerization(ae55170e-8c06-48f6-ba96-7389d7ee4841).html