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Dynamical theory of activated processes in globular proteins
- Source :
- Proceedings of the National Academy of Sciences of the United States of America. 79(13)
- Publication Year :
- 1982
-
Abstract
- A method is described for calculating the reaction rate in globular proteins of activated processes such as ligand binding or enzymatic catalysis. The method is based on the determination of the probability that the system is in the transition state and of the magnitude of the reactive flux for transition-state systems. An "umbrella sampling" simulation procedure is outlined for evaluating the transition-state probability. The reactive flux is obtained from an approach described previously for calculating the dynamics of transition-state trajectories. An application to the rotational isomerization of an aromatic ring in the bovine pancreatic trypsin inhibitor is presented. The results demonstrate the feasibility of calculating rate constants for reactions in proteins and point to the importance of solvent effects for reactions that occur near the protein surface.
- Subjects :
- chemistry.chemical_classification
Quantitative Biology::Biomolecules
Multidisciplinary
Chemical Phenomena
Chemistry
Globular protein
Chemistry, Physical
Protein Conformation
Quantitative Biology::Molecular Networks
Proteins
Models, Biological
Enzyme catalysis
Reaction rate
Quantitative Biology::Subcellular Processes
Reaction rate constant
Protein structure
Computational chemistry
Chemical physics
Solvent effects
Umbrella sampling
Physics::Chemical Physics
Flux (metabolism)
Mathematics
Research Article
Subjects
Details
- ISSN :
- 00278424
- Volume :
- 79
- Issue :
- 13
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Accession number :
- edsair.doi.dedup.....1d5d5f64979709f4a76a5d548fe99eb4