Evidence map›Paper›PMID 21651308›Full record

ArticleOrganic letters2011

Environment- and sequence-dependence of helical type in membrane-spanning peptides composed of β3-amino acids.

Ivan V Korendovych, Scott J Shandler, Geronda L Montalvo, William F DeGrado

Erratum issuedAbstract read
In one paragraph

Article in Organic letters, 2011. 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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Catalytic peptide assemblies.Chemical Society reviews · 2018
    Review
  2. Article
  3. α-Helix mimicry with α/β-peptides.Methods in enzymology · 2013
    Article
  4. Computational design of a β-peptide that targets transmembrane helices.Journal of the American Chemical Society · 2011
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors.

Ivan V KorendovychDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Scott J Shandler
Geronda L Montalvo
William F DeGrado

Funding

Structure of M2 Proton Channel from Influenza A VirusR01GM056423 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1997 to 2016
$4.5M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
NIGMS NIH HHS GM54616NIGMS NIH HHS GM56423NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM056423NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

Transmembrane (TM) β-peptides comprised of acyclic β(3)-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β(3)-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β(3)-substituted acyclic β-peptides has practical implications for foldamer design, as it suggests that both the 14-helix and 12-helix might be reasonable platforms for molecular recognition.

Indexed as

Amino AcidsAmino Acid SequenceModels, MolecularMolecular Sequence DataPeptidesProtein Structure, SecondaryStereoisomerismAmino AcidsPeptides

Identifiers

PMID21651308
PMCPMC3124938

What OpenQuestion holds

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LicenceTDM
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.