Evidence map›Paper›PMID 23039617›Full record

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.

Nicholas Greives, Huan-Xiang Zhou

Open access · bronzeAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Theoretical frameworks for multiscale modeling and simulation.Current opinion in structural biology · 2014
    Review
  7. Modeling protein association mechanisms and kinetics.Current opinion in structural biology · 2013
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Nicholas GreivesDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
Huan-Xiang Zhou
Florida State University · US

Funding

THEORY OF PROTEIN/PROTEIN ASSOCIATIONR01GM058187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 1998 to 2016
$3.7M
NIGMS NIH HHS GM58187NIGMS NIH HHS R01 GM058187
6 · The paper itself

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.

Indexed as

Molecular Dynamics SimulationBinding SitesKineticsLigandsPliabilityProteinsLigandsProteins

Identifiers

PMID23039617
PMCPMC3477184
OpenAlexW1999773220

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.