Evidence map›Paper›PMID 22566663›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Shifting hydrogen bonds may produce flexible transmembrane helices.

Zheng Cao, James U Bowie

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022
    Review
  6. Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  7. Review
  8. Diverse Scientific Benchmarks for Implicit Membrane Energy Functions.Journal of chemical theory and computation · 2021
    Article
  9. Article
  10. Article
  11. Quantitative Analysis of Multiplex H-Bonds.Journal of the American Chemical Society · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Helical Structure of Recombinant Melittin.The journal of physical chemistry. B · 2019
    Article
  17. Article
  18. Bicelle size modulates the rate of bacteriorhodopsin folding.Protein science : a publication of the Protein Society · 2018
    Article
  19. Article
  20. Article
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

2 authors.

Zheng CaoDepartment of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, University of California, Boyer Hall, 611 Charles E. Young Drive East, Los Angeles, CA 90095, USA.
James U Bowie

Funding

Membrane Protein StabilityR01GM063919 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BOWIE, JAMES U · 2001 to 2021
$5.6M
NIGMS NIH HHS R01 GM063919NIGMS NIH HHS R01GM063919
6 · The paper itself

Abstract

The intricate functions of membrane proteins would not be possible without bends or breaks that are remarkably common in transmembrane helices. The frequent helix distortions are nevertheless surprising because backbone hydrogen bonds should be strong in an apolar membrane, potentially rigidifying helices. It is therefore mysterious how distortions can be generated by the evolutionary currency of random point mutations. Here we show that we can engineer a transition between distinct distorted helix conformations in bacteriorhodopsin with a single-point mutation. Moreover, we estimate the energetic cost of the conformational transitions to be smaller than 1 kcal/mol. We propose that the low energy of distortion is explained in part by the shifting of backbone hydrogen bonding partners. Consistent with this view, extensive backbone hydrogen bond shifts occur during helix conformational changes that accompany functional cycles. Our results explain how evolution has been able to liberally exploit transmembrane helix bending for the optimization of membrane protein structure, function, and dynamics.

Indexed as

Protein FoldingBacteriorhodopsinsCrystallography, X-RayEvolution, MolecularHalobacteriumHydrogen BondingMembrane ProteinsPoint MutationProlineProtein Structure, SecondaryThermodynamicsBacteriorhodopsinsMembrane ProteinsProline

Identifiers

PMID22566663
PMCPMC3361389
OpenAlexW2127395373

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.