Evidence map›Paper›PMID 21415366›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Unsuspected pathway of the allosteric transition in hemoglobin.

Stefan Fischer, Kenneth W Olsen, Kwangho Nam, Martin Karplus

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 77 citations in OpenAlex.

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  17. The allosteric switching mechanism in bacteriophage MS2.The Journal of chemical physics · 2016
    Article
  18. Two pathways mediate interdomain allosteric regulation in pin1.Structure (London, England : 1993) · 2015
    Article
  19. Review
  20. 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

4 authors at 4 institutions in 3 countries.

Stefan FischerInterdisziplinäres Zentrum für Wissenschaftliches Rechnen-Computational Biochemistry, Im Neuenheimer Feld 368, University of Heidelberg, D-69120 Heidelberg, Germany. stefan.fischer@iwr.uni-heidelberg.de
Kenneth W Olsen
Kwangho Nam
Martin Karplus
Harvard University · USHeidelberg University · DEInstitut de Science et d'Ingénierie Supramoléculaires · FRLoyola University Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Large conformational transitions play an essential role in the function of many proteins, but experiments do not provide the atomic details of the path followed in going from one end structure to the other. For the hemoglobin tetramer, the transition path between the unliganded (T) and tetraoxygenated (R) structures is not known, which limits our understanding of the cooperative mechanism in this classic allosteric system, where both tertiary and quaternary changes are involved. The conjugate peak refinement algorithm is used to compute an unbiased minimum energy path at atomic detail between the two end states. Although the results confirm some of the proposals of Perutz [Perutz MF (1970) Stereochemistry of cooperative effects in haemoglobin. Nature 228:726-734], the subunit motions do not follow the textbook description of a simple rotation of one αβ-dimer relative to the other. Instead, the path consists of two sequential quaternary rotations, each involving different subdomains and axes. The quaternary transitions are preceded and followed by phases of tertiary structural changes. The results explain the recent photodissociation measurements, which suggest that the quaternary transition has a fast (2 μs) as well as a slow (20 μs) component and provide a testable model for single molecule FRET experiments.

Indexed as

Models, ChemicalModels, MolecularProtein ConformationAllosteric RegulationHemoglobinsProtein SubunitsHemoglobinsProtein Subunits

Identifiers

PMID21415366
PMCPMC3078355
OpenAlexW2042964041

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.