Evidence map›Paper›PMID 24600446›Full record

ArticleFrontiers in microbiology2014

An experimental point of view on hydration/solvation in halophilic proteins.

Romain Talon, Nicolas Coquelle, Dominique Madern, Eric Girard

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  3. Determination ofJournal of the Royal Society, Interface · 2025
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  10. Experimental study of proteome halophilicity using nanoDSF: a proof of concept.Extremophiles : life under extreme conditions · 2021
    Article
  11. Article
  12. NewFrontiers in microbiology · 2019
    Article
  13. Polypentagonal ice-like water networks emerge solely in an activity-improved variant of ice-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2018
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  14. 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

4 authors at 2 institutions in 1 country.

Romain TalonInstitut de Biologie Structurale, Université Grenoble Alpes Grenoble, France ; CEA, DSV, Institut de Biologie Structurale Grenoble, France ; Institut de Biologie Structurale, Centre National de la Recherche Scientifique Grenoble, France.
Nicolas CoquelleInstitut de Biologie Structurale, Université Grenoble Alpes Grenoble, France ; CEA, DSV, Institut de Biologie Structurale Grenoble, France ; Institut de Biologie Structurale, Centre National de la Recherche Scientifique Grenoble, France.
Dominique MadernInstitut de Biologie Structurale, Université Grenoble Alpes Grenoble, France ; CEA, DSV, Institut de Biologie Structurale Grenoble, France ; Institut de Biologie Structurale, Centre National de la Recherche Scientifique Grenoble, France.
Eric GirardInstitut de Biologie Structurale, Université Grenoble Alpes Grenoble, France ; CEA, DSV, Institut de Biologie Structurale Grenoble, France ; Institut de Biologie Structurale, Centre National de la Recherche Scientifique Grenoble, France.
CEA Grenoble · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-solvent interactions govern the behaviors of proteins isolated from extreme halophiles. In this work, we compared the solvent envelopes of two orthologous tetrameric malate dehydrogenases (MalDHs) from halophilic and non-halophilic bacteria. The crystal structure of the MalDH from the non-halophilic bacterium Chloroflexus aurantiacus (Ca MalDH) solved, de novo, at 1.7 Å resolution exhibits numerous water molecules in its solvation shell. We observed that a large number of these water molecules are arranged in pentagonal polygons in the first hydration shell of Ca MalDH. Some of them are clustered in large networks, which cover non-polar amino acid surface. The crystal structure of MalDH from the extreme halophilic bacterium Salinibacter ruber (Sr) solved at 1.55 Å resolution shows that its surface is strongly enriched in acidic amino acids. The structural comparison of these two models is the first direct observation of the relative impact of acidic surface enrichment on the water structure organization between a halophilic protein and its non-adapted counterpart. The data show that surface acidic amino acids disrupt pentagonal water networks in the hydration shell. These crystallographic observations are discussed with respect to halophilic protein behaviors in solution.

Indexed as

acidic proteinsadaptationhalophilichydrationmalate dehydrogenasesalinibactersolvationwater pentagon

Identifiers

PMID24600446
PMCPMC3930881
OpenAlexW2074802501

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.