ArticleF1000Research2015
Molecular Dynamics Simulations of the Temperature Induced Unfolding of Crambin Follow the Arrhenius Equation.
Article in F1000Research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Temperature-Dependent Active-Site Rearrangements of PETaseSM14: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- PEPCONF, a diverse data set of peptide conformational energies.Scientific data · 2019Article
- Investigation of net unidirectional ring shuttling in a chemically fueled [2]catenane.Journal of molecular modeling · 2018Article
- Validation of Molecular Dynamics Simulations for Prediction of Three-Dimensional Structures of Small Proteins.Molecules (Basel, Switzerland) · 2017Article
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Authors and funding
2 authors.
Funding
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Abstract
Molecular dynamics simulations have been used extensively to model the folding and unfolding of proteins. The rates of folding and unfolding should follow the Arrhenius equation over a limited range of temperatures. This study shows that molecular dynamic simulations of the unfolding of crambin between 500K and 560K do follow the Arrhenius equation. They also show that while there is a large amount of variation between the simulations the average values for the rate show a very high degree of correlation.
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