Evidence map›Paper›PMID 31705614›Full record

ArticleChembiochem : a European journal of chemical biology2020

Rapid Biophysical Characterization and NMR Spectroscopy Structural Analysis of Small Proteins from Bacteria and Archaea.

Nina Kubatova, Dennis J Pyper, Hendrik R A Jonker, Krishna Saxena, Laura Remmel, Christian Richter, Sabine Brantl, Elena Evguenieva-Hackenberg, Wolfgang R Hess, Gabriele Klug and 8 more

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. 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
1.6field-weighted citation impact, top 16% 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, 34 citations in OpenAlex.

  1. Review
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  5. C(P)XCG Proteins ofInternational journal of molecular sciences · 2024
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  13. Small Proteins; Big Questions.Journal of bacteriology · 2022
    Article
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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

18 authors at 9 institutions in 3 countries.

Nina KubatovaInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
Dennis J PyperInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
Hendrik R A JonkerInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
Krishna SaxenaInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
Laura RemmelInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
Christian RichterInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.
Sabine BrantlAG Bakteriengenetik, Matthias-Schleiden-Institut, Philosophenweg 12, 07743, Jena, Germany.
Elena Evguenieva-HackenbergInstitute for Microbiology and Molecular Biology, Justus Liebig University Giessen, Heinrich-Buff-Ring 26, 35392, Giessen, Germany.
Wolfgang R HessFaculty of Biology, Genetics and Experimental Bioinformatics, Albert Ludwigs University Freiburg, Schänzlestrasse 1, 79104, Freiburg, Germany.
Gabriele KlugInstitute for Microbiology and Molecular Biology, Justus Liebig University Giessen, Heinrich-Buff-Ring 26, 35392, Giessen, Germany.
Anita MarchfelderBiologie II, Ulm University, Albert-Einstein-Allee 11, 89069, Ulm, Germany.
Jörg SoppaInstitute for Molecular Biosciences, Johann Wolfgang Goethe University, Max-von-Laue-Strasse 9, 60438, Frankfurt am Main, Germany.
Wolfgang StreitDepartment of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609, Hamburg, Germany.
Maxim MayzelSwedish NMR Centre, University of Gothenburg, P. O. Box 465, 40530, Gothenburg, Sweden.
Vladislav Y OrekhovSwedish NMR Centre, University of Gothenburg, P. O. Box 465, 40530, Gothenburg, Sweden.
Monika FuxreiterMTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Nagyerdei krt 98, 4032, Debrecen, Hungary.
Ruth A SchmitzInstitute for General Microbiology, Christian Albrechts University Kiel, Am Botanischen Garten 1-9, 24118, Kiel, Germany.
Harald SchwalbeInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Strasse 7, 60438, Frankfurt/Main, Germany.ORCID 0000-0001-5693-7909
Goethe University Frankfurt · DEJustus-Liebig-Universität Gießen · DEUniversity of Gothenburg · SEChristian-Albrechts-Universität zu Kiel · DEInstitute for Sports Medicine · DEUniversität Hamburg · DEUniversität Ulm · DEUniversity of Debrecen · HUUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins encoded by small open reading frames (sORFs) have a widespread occurrence in diverse microorganisms and can be of high functional importance. However, due to annotation biases and their technically challenging direct detection, these small proteins have been overlooked for a long time and were only recently rediscovered. The currently rapidly growing number of such proteins requires efficient methods to investigate their structure-function relationship. Herein, a method is presented for fast determination of the conformational properties of small proteins. Their small size makes them perfectly amenable for solution-state NMR spectroscopy. NMR spectroscopy can provide detailed information about their conformational states (folded, partially folded, and unstructured). In the context of the priority program on small proteins funded by the German research foundation (SPP2002), 27 small proteins from 9 different bacterial and archaeal organisms have been investigated. It is found that most of these small proteins are unstructured or partially folded. Bioinformatics tools predict that some of these unstructured proteins can potentially fold upon complex formation. A protocol for fast NMR spectroscopy structure elucidation is described for the small proteins that adopt a persistently folded structure by implementation of new NMR technologies, including automated resonance assignment and nonuniform sampling in combination with targeted acquisition.

Indexed as

Protein FoldingArchaeaArchaeal ProteinsBacteriaBacterial ProteinsComputational BiologyNuclear Magnetic Resonance, BiomolecularOpen Reading FramesProtein ConformationArchaeal ProteinsBacterial ProteinsNMR spectroscopyproteomicssmall proteinsstructural biologystructure-activity relationships

Identifiers

PMID31705614
PMCPMC7217052
OpenAlexW2987821228

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.