Evidence map›Paper›PMID 30285440›Full record

ArticleThe journal of physical chemistry. B2018

Dynamics of Quaternary Structure Transitions in R-State Carbonmonoxyhemoglobin Unveiled in Time-Resolved X-ray Scattering Patterns Following a Temperature Jump.

Hyun Sun Cho, Friedrich Schotte, Valentyn Stadnytskyi, Anthony DiChiara, Robert Henning, Philip Anfinrud

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

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  10. Time-resolved X-ray scattering studies of proteins.Current opinion in structural biology · 2021
    Review
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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

6 authors at 3 institutions in 1 country.

Hyun Sun ChoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases , National Institutes of Health , Bethesda , Maryland 220892-0520 , United States.
Friedrich SchotteLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases , National Institutes of Health , Bethesda , Maryland 220892-0520 , United States.
Valentyn StadnytskyiLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases , National Institutes of Health , Bethesda , Maryland 220892-0520 , United States.
Anthony DiChiaraArgonne National Laboratory , 9700 S. Cass Ave. , Argonne , Illinois 60439 , United States.
Robert HenningCenter for Advanced Radiation Sources , University of Chicago , Chicago , Illinois 60637 , United States.
Philip AnfinrudLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases , National Institutes of Health , Bethesda , Maryland 220892-0520 , United States.ORCID 0000-0002-8261-0624
National Institutes of Health · USArgonne National Laboratory · USUniversity of Chicago · US

Funding

Ultrafast Biophysical Studies of Proteins: Time-resolved Laue crystallographyZIADK029058 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2009 to 2025
$9.3M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
Intramural NIH HHS ZIA DK029058NIGMS NIH HHS R24 GM111072
6 · The paper itself

Abstract

It is well-known that tetrameric hemoglobin binds ligands cooperatively by undergoing a ligand-induced T → R quaternary structure transition, a structure-function relationship that has long served as a model system for understanding allostery in proteins. However, kinetic studies of the reverse, R → T quaternary structure transition following photolysis of carbonmonoxyhemoglobin (HbCO) reveal complex behavior that may be better explained by the presence of two different R quaternary structures coexisting in thermal equilibrium. Indeed, we report here time-resolved small- and wide-angle X-ray scattering (SAXS/WAXS) patterns of HbCO following a temperature jump that not only provide unambiguous evidence for more than one R state, but also unveil the time scale for interconversion between them. Since the time scale for the photolysis-induced R → T transition is likely different for different R-states, this structural heterogeneity must be accounted for to properly explain the kinetic heterogeneity observed in time-resolved spectroscopic studies following photolysis of HbCO.

Indexed as

Molecular Dynamics SimulationTemperatureCarboxyhemoglobinErythrocytesHumansKineticsProtein ConformationScattering, Small AngleTime FactorsX-Ray DiffractionCarboxyhemoglobin

Identifiers

PMID30285440
PMCPMC6580858
OpenAlexW2895341905

What OpenQuestion holds

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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.