ArticleThe Journal of chemical physics2012
BDflex: a method for efficient treatment of molecular flexibility in calculating protein-ligand binding rate constants from brownian dynamics simulations.
Article in The Journal of chemical physics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 15 citations in OpenAlex.
- Brownian Dynamics Simulations of Biological Molecules.Trends in chemistry · 2019Article
- Structural and dynamic basis of substrate permissiveness in hydroxycinnamoyltransferase (HCT).PLoS computational biology · 2018Article
- Rate Constants and Mechanisms of Protein-Ligand Binding.Annual review of biophysics · 2017Review
- Multiscale Estimation of Binding Kinetics Using Brownian Dynamics, Molecular Dynamics and Milestoning.PLoS computational biology · 2015Article
- Substrate tunnels in enzymes: structure-function relationships and computational methodology.Proteins · 2015Review
- Theoretical frameworks for multiscale modeling and simulation.Current opinion in structural biology · 2014Review
- Modeling protein association mechanisms and kinetics.Current opinion in structural biology · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
A method developed by Northrup et al. [J. Chem. Phys. 80, 1517 (1984)] for calculating protein-ligand binding rate constants (k(a)) from brownian dynamics (BD) simulations has been widely used for rigid molecules. Application to flexible molecules is limited by the formidable computational cost to treat conformational fluctuations during the long BD simulations necessary for k(a) calculation. Here, we propose a new method called BDflex for k(a) calculation that circumvents this problem. The basic idea is to separate the whole space into an outer region and an inner region, and formulate k(a) as the product of k(E) and η(d), which are obtained by separately solving exterior and interior problems. k(E) is the diffusion-controlled rate constant for the ligand in the outer region to reach the dividing surface between the outer and inner regions; in this exterior problem conformational fluctuations can be neglected. η(d) is the probability that the ligand, starting from the dividing surface, will react at the binding site rather than escape to infinity. The crucial step in reducing the determination of η(d) to a problem confined to the inner region is a radiation boundary condition imposed on the dividing surface; the reactivity on this boundary is proportional to k(E). By confining the ligand to the inner region and imposing the radiation boundary condition, we avoid multiple-crossing of the dividing surface before reaction at the binding site and hence dramatically cut down the total simulation time, making the treatment of conformational fluctuations affordable. BDflex is expected to have wide applications in problems where conformational fluctuations of the molecules are crucial for productive ligand binding, such as in cases where transient widening of a bottleneck allows the ligand to access the binding pocket, or the binding site is properly formed only after ligand entrance induces the closure of a lid.
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