Evidence map›Paper›PMID 26771248›Full record

ArticleeLife2016

α/β coiled coils.

Marcus D Hartmann, Claudia T Mendler, Jens Bassler, Ioanna Karamichali, Oswin Ridderbusch, Andrei N Lupas, Birte Hernandez Alvarez

Abstract read
In one paragraph

Article in eLife, 2016. 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
–field-weighted citation impact
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.

  1. Review
  2. Helical substructures of 4D constructions that determine the structure of α-helices.Acta crystallographica. Section A, Foundations and advances · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Characterisation of sequence-structure-function space in sensor-effector integrators of phytochrome-regulated diguanylate cyclases.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  7. A multidomain connector links the outer membrane and cell wall in phylogenetically deep-branching bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Coiled-coils: The long and short of it.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  19. Preface.Methods in enzymology · 2016
    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

7 authors.

Marcus D HartmannDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID http://orcid.org/0000-0001-6937-5677
Claudia T MendlerDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Jens BasslerDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Ioanna KaramichaliDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Oswin RidderbuschDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Andrei N LupasDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID http://orcid.org/0000-0002-1959-4836
Birte Hernandez AlvarezDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coiled coils are the best-understood protein fold, as their backbone structure can uniquely be described by parametric equations. This level of understanding has allowed their manipulation in unprecedented detail. They do not seem a likely source of surprises, yet we describe here the unexpected formation of a new type of fiber by the simple insertion of two or six residues into the underlying heptad repeat of a parallel, trimeric coiled coil. These insertions strain the supercoil to the breaking point, causing the local formation of short β-strands, which move the path of the chain by 120° around the trimer axis. The result is an α/β coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold.

Indexed as

Amino Acid SequenceBacterial ProteinsCrystallography, X-RayGram-Positive BacteriaHydrogen BondingModels, MolecularProtein Structure, SecondaryProtein Structure, TertiaryBacterial Proteinsbiophysicsfiberheptad repeatnonesequence periodicitystructural biologysupercoilα-helix

Identifiers

PMID26771248
PMCPMC4786415

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.