Evidence map›Paper›PMID 21985970›Full record

ReviewFEBS letters2012

Proteins as strongly correlated protonic systems.

Vernon Couch, Alexei Stuchebrukhov

Abstract readReview
In one paragraph

Review in FEBS letters, 2012. 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
–field-weighted citation impact
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.

  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.

Vernon CouchDepartment of Chemistry, University of California, Davis, CA 95616, USA.
Alexei Stuchebrukhov

Funding

Theoretical Study of Charge Transfer in Cytochrome C OxidaseR01GM054052 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STUCHEBRUKHOV, ALEXEI A · 2002 to 2021
$3.3M
THEORETICAL STUDY OF BIOLOGICAL ELECTRON TRANSFERR29GM054052 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STUCHEBRUKHOV, ALEXEI A · 1996 to 2000
$101k
NIGMS NIH HHS GM54052NIGMS NIH HHS R01 GM054052NIGMS NIH HHS R29 GM054052
6 · The paper itself

Abstract

Determination of the protonation state of enzymes is a challenging problem in computational biophysics largely due to the vast number of possible protonic configurations. The protonation state dynamics of respiratory complex I was investigated via Monte Carlo and asynchronous dynamics simulations and a novel eigenvector analysis. Many low lying states were identified and examined. The analysis revealed that the protonic states form a quasi-continuous band of energies, which are highly correlated and inhomogeneous. Many states have similar energies, but differ significantly in their protonic composition. In order to transfer from one such state to another, a large number of protons should be exchanged simultaneously raising the question of the ergodicity of protonation dynamics of such systems.

Indexed as

Models, ChemicalMonte Carlo MethodProtonsAlgorithmsComputer SimulationElectron Transport Complex IProteinsThermodynamicsElectron Transport Complex IProteinsProtons

Identifiers

PMID21985970
PMCPMC4220737

What OpenQuestion holds

Textmetadata
LicenceTDM
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.