Evidence map›Paper›PMID 25664692›Full record

ArticleNature chemical biology2015

Local and macroscopic electrostatic interactions in single α-helices.

Emily G Baker, Gail J Bartlett, Matthew P Crump, Richard B Sessions, Noah Linden, Charl F J Faul, Derek N Woolfson

Erratum issuedAbstract read
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
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  5. Chemical science · 2025
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  7. How Rigid Are Anthranilamide Molecular Electrets?The journal of physical chemistry. B · 2025
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  11. Article
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  16. Uncovering the Contributions of Charge Regulation to the Stability of Single Alpha Helices.Chemphyschem : a European journal of chemical physics and physical chemistry · 2023
    Article
  17. Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Emily G BakerSchool of Chemistry, University of Bristol, Bristol, UK.
Gail J BartlettSchool of Chemistry, University of Bristol, Bristol, UK.
Matthew P CrumpSchool of Chemistry, University of Bristol, Bristol, UK.
Richard B SessionsSchool of Biochemistry, University of Bristol, Bristol, UK.
Noah LindenSchool of Mathematics, University of Bristol, Bristol, UK.
Charl F J FaulSchool of Chemistry, University of Bristol, Bristol, UK.
Derek N Woolfson1] School of Chemistry, University of Bristol, Bristol, UK. [2] School of Biochemistry, University of Bristol, Bristol, UK.

Funding

Wellcome Trust 082352
6 · The paper itself

Abstract

The noncovalent forces that stabilize protein structures are not fully understood. One way to address this is to study equilibria between unfolded states and α-helices in peptides. Electrostatic forces-which include interactions between side chains, the backbone and side chains, and side chains and the helix macrodipole-are believed to contribute to these equilibria. Here we probe these interactions experimentally using designed peptides. We find that both terminal backbone-side chain and certain side chain-side chain interactions (which include both local effects between proximal charges and interatomic contacts) contribute much more to helix stability than side chain-helix macrodipole electrostatics, which are believed to operate at larger distances. This has implications for current descriptions of helix stability, the understanding of protein folding and the refinement of force fields for biomolecular modeling and simulations. In addition, this study sheds light on the stability of rod-like structures formed by single α-helices, which are common in natural proteins such as non-muscle myosins.

Indexed as

Protein Structure, SecondaryStatic ElectricityAmino Acid SequenceComputational BiologyGlutamic AcidLysineModels, MolecularMolecular Sequence DataMyosinsPeptidesProtein FoldingProtein UnfoldingGlutamic AcidLysineMyosinsPeptides

Identifiers

PMID25664692
PMCPMC4668598

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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.