Evidence map›Paper›PMID 24969589›Full record

ArticleJournal of the American Chemical Society2014

Specific and nonspecific interactions in ultraweak protein-protein associations revealed by solvent paramagnetic relaxation enhancements.

Helle Johansson, Malene Ringkjøbing Jensen, Henrik Gesmar, Sebastian Meier, Joachim M Vinther, Camille Keeler, Michael E Hodsdon, Jens J Led

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  6. Activation mechanism of the μ-opioid receptor by an allosteric modulator.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  9. 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

8 authors at 4 institutions in 4 countries.

Helle JohanssonDepartment of Chemistry, University of Copenhagen , Universitetsparken 5, DK-2100 Copenhagen Ø, Denmark.
Malene Ringkjøbing Jensen
Henrik Gesmar
Sebastian Meier
Joachim M Vinther
Camille Keeler
Michael E Hodsdon
Jens J Led
University of Copenhagen · DKYale University · USInstitut de Biologie Structurale · FRUniversity of Stuttgart · DE

Funding

Structural Basis of Prolactin Receptor RecognitionR01CA108992 · NCI · YALE UNIVERSITY · PI HODSDON, MICHAEL E · 2005 to 2009
$1.4M
NCI NIH HHS R01 CA108992NCI NIH HHS R01CA108992
6 · The paper itself

Abstract

Weak and transient protein-protein interactions underlie numerous biological processes. However, the location of the interaction sites of the specific complexes and the effect of transient, nonspecific protein-protein interactions often remain elusive. We have investigated the weak self-association of human growth hormone (hGH, KD = 0.90 ± 0.03 mM) at neutral pH by the paramagnetic relaxation enhancement (PRE) of the amide protons induced by the soluble paramagnetic relaxation agent, gadodiamide (Gd(DTPA-BMA)). Primarily, it was found that the PREs are in agreement with the general Hwang-Freed model for relaxation by translational diffusion (J. Chem. Phys. 1975, 63, 4017-4025), only if crowding effects on the diffusion in the protein solution are taken into account. Second, by measuring the PREs of the amide protons at increasing hGH concentrations and a constant concentration of the relaxation agent, it is shown that a distinction can be made between residues that are affected only by transient, nonspecific protein-protein interactions and residues that are involved in specific protein-protein associations. Thus, the PREs of the former residues increase linearly with the hGH concentration in the entire concentration range because of a reduction of the diffusion caused by the transient, nonspecific protein-protein interactions, while the PREs of the latter residues increase only at the lower hGH concentrations but decrease at the higher concentrations because of specific protein-protein associations that impede the access of gadodiamide to the residues of the interaction surface. Finally, it is found that the ultraweak aggregation of hGH involves several interaction sites that are located in patches covering a large part of the protein surface.

Indexed as

Gadolinium DTPAHuman Growth HormoneModels, ChemicalModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein MultimerizationProtonsSolventsgadodiamideGadolinium DTPAHuman Growth HormoneProtonsSolvents

Identifiers

PMID24969589
PMCPMC4111215
OpenAlexW2312809908

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.