Evidence map›Paper›PMID 22696485›Full record

ArticleJournal of the Royal Society, Interface2012

Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics.

A M Stadler, C J Garvey, A Bocahut, S Sacquin-Mora, I Digel, G J Schneider, F Natali, G M Artmann, G Zaccai

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Journal of the Royal Society, Interface, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

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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

9 authors at 5 institutions in 3 countries.

A M StadlerInstitute for Complex Systems (ICS-5: Molecular Biophysics), Forschungszentrum Jülich, Jülich, Germany. a.stadler@fz-juelich.de
C J Garvey
A Bocahut
S Sacquin-Mora
I Digel
G J Schneider
F Natali
G M Artmann
G Zaccai
FH Aachen · DEForschungszentrum Jülich · DEInstitut Laue-Langevin · FRSorbonne Université · FRAustralian Nuclear Science and Technology Organisation · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermodynamic stability, configurational motions and internal forces of haemoglobin (Hb) of three endotherms (platypus, Ornithorhynchus anatinus; domestic chicken, Gallus gallus domesticus and human, Homo sapiens) and an ectotherm (salt water crocodile, Crocodylus porosus) were investigated using circular dichroism, incoherent elastic neutron scattering and coarse-grained Brownian dynamics simulations. The experimental results from Hb solutions revealed a direct correlation between protein resilience, melting temperature and average body temperature of the different species on the 0.1 ns time scale. Molecular forces appeared to be adapted to permit conformational fluctuations with a root mean square displacement close to 1.2 Å at the corresponding average body temperature of the endotherms. Strong forces within crocodile Hb maintain the amplitudes of motion within a narrow limit over the entire temperature range in which the animal lives. In fully hydrated powder samples of human and chicken, Hb mean square displacements and effective force constants on the 1 ns time scale showed no differences over the whole temperature range from 10 to 300 K, in contrast to the solution case. A complementary result of the study, therefore, is that one hydration layer is not sufficient to activate all conformational fluctuations of Hb in the pico- to nanosecond time scale which might be relevant for biological function. Coarse-grained Brownian dynamics simulations permitted to explore residue-specific effects. They indicated that temperature sensing of human and chicken Hb occurs mainly at residues lining internal cavities in the β-subunits.

Indexed as

Protein ConformationTemperatureAdaptation, BiologicalAlligators and CrocodilesAmino Acid SequenceAnimalsBody TemperatureChickensCircular DichroismComputational BiologyComputer SimulationHemoglobinsHumansMolecular Sequence DataNeutron DiffractionPlatypusHemoglobins

Identifiers

PMID22696485
PMCPMC3479923
OpenAlexW2170900800

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.