Evidence map›Paper›PMID 34078890›Full record

ArticleNature communications2021

Through bonds or contacts? Mapping protein vibrational energy transfer using non-canonical amino acids.

Erhan Deniz, Luis Valiño-Borau, Jan G Löffler, Katharina B Eberl, Adnan Gulzar, Steffen Wolf, Patrick M Durkin, Robert Kaml, Nediljko Budisa, Gerhard Stock and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

13 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Versatile Vibrational Energy Sensors for Proteins.Angewandte Chemie (International ed. in English) · 2022
    Article
  11. Article
  12. Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.Chembiochem : a European journal of chemical biology · 2022
    Review
  13. Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021
    Review
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

11 authors at 4 institutions in 3 countries.

Erhan Deniz *Institute of Biophysics, Goethe University Frankfurt, Frankfurt/Main, Germany.ORCID 0000-0002-6890-2989
Luis Valiño-Borau *Biomolecular Dynamics, Institute of Physics, Albert Ludwigs University, Freiburg, Germany.ORCID 0000-0001-6560-505X
Jan G Löffler *Institute of Biophysics, Goethe University Frankfurt, Frankfurt/Main, Germany.ORCID 0000-0003-4085-592X
Katharina B EberlInstitute of Biophysics, Goethe University Frankfurt, Frankfurt/Main, Germany.
Adnan GulzarBiomolecular Dynamics, Institute of Physics, Albert Ludwigs University, Freiburg, Germany.
Steffen WolfBiomolecular Dynamics, Institute of Physics, Albert Ludwigs University, Freiburg, Germany.ORCID 0000-0003-1752-6175
Patrick M DurkinInstitute of Chemistry, Technical University Berlin, Berlin, Germany.
Robert KamlInstitute of Chemistry, Technical University Berlin, Berlin, Germany.
Nediljko BudisaInstitute of Chemistry, Technical University Berlin, Berlin, Germany.ORCID 0000-0001-8437-7304
Gerhard StockBiomolecular Dynamics, Institute of Physics, Albert Ludwigs University, Freiburg, Germany. stock@physik.uni-freiburg.de.ORCID 0000-0002-3302-3044
Jens BredenbeckInstitute of Biophysics, Goethe University Frankfurt, Frankfurt/Main, Germany. bredenbeck@biophysik.uni-frankfurt.de.ORCID 0000-0003-1929-9092
Goethe University Frankfurt · DEUniversity of Freiburg · DETechnische Universität Berlin · DEGeosyntec Consultants (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vibrational energy transfer (VET) is essential for protein function. It is responsible for efficient energy dissipation in reaction sites, and has been linked to pathways of allosteric communication. While it is understood that VET occurs via backbone as well as via non-covalent contacts, little is known about the competition of these two transport channels, which determines the VET pathways. To tackle this problem, we equipped the β-hairpin fold of a tryptophan zipper with pairs of non-canonical amino acids, one serving as a VET injector and one as a VET sensor in a femtosecond pump probe experiment. Accompanying extensive non-equilibrium molecular dynamics simulations combined with a master equation analysis unravel the VET pathways. Our joint experimental/computational endeavor reveals the efficiency of backbone vs. contact transport, showing that even if cutting short backbone stretches of only 3 to 4 amino acids in a protein, hydrogen bonds are the dominant VET pathway.

Indexed as

AlanineAllosteric RegulationAzulenesEnergy TransferHydrogen BondingMolecular Dynamics SimulationProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProteinsQuantum TheorySolutionsThermodynamicsTryptophanVibrationAlanineAzulenesProteinsSolutionsTrpzip2 proteinTryptophan

Identifiers

PMID34078890
PMCPMC8172543
OpenAlexW3165860780

What OpenQuestion holds

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LicenceCC BY
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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.