Evidence map›Paper›PMID 33877634›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Molecular Dynamics-Based Thermodynamic and Kinetic Characterization of Membrane Protein Conformational Transitions.

Dylan Ogden, Mahmoud Moradi

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
2.6field-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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. Article
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.

Dylan OgdenDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA.
Mahmoud MoradiDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA. moradi@uark.edu.
University of Arkansas at Fayetteville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular dynamics (MD) simulations are routinely used to study structural dynamics of membrane proteins. However, conventional MD is often unable to sample functionally important conformational transitions of membrane proteins such as those involved in active membrane transport or channel activation process. Here we describe a combination of multiple MD based techniques that allows for a rigorous characterization of energetics and kinetics of large-scale conformational changes in membrane proteins. The methodology is based on biased, nonequilibrium, collective-variable based simulations including nonequilibrium pulling, string method with swarms of trajectories, bias-exchange umbrella sampling, and rate estimation techniques.

Indexed as

Computational BiologyKineticsMembrane ProteinsModels, MolecularMolecular Dynamics SimulationProtein ConformationThermodynamicsMembrane ProteinsConformational LandscapeMembrane ProteinNonequilibrium PullingOrientation QuaternionString MethodTransition Rate EstimationUmbrella Sampling

Identifiers

PMID33877634
OpenAlexW3152790820

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.