Evidence map›Paper›PMID 25974390›Full record

ArticleJournal of the American Chemical Society2015

Heterogeneous H-bonding in a foldamer helix.

Brian F Fisher, Li Guo, Brian S Dolinar, Ilia A Guzei, Samuel H Gellman

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Do calmodulin binding IQ motifs have built-in capping domains?Protein science : a publication of the Protein Society · 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

5 authors.

Brian F FisherDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Li GuoDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Brian S DolinarDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Ilia A GuzeiDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Samuel H GellmanDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

Funding

MALDI TOF/TOF Mass SpectrometerS10RR024601 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 2008 to 2008
$376k
PURCHASE OF A 1409 TESLA NMR INSTRUMENTS10RR013866 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI GELLMAN, SAMUEL H. · 1999 to 1999
–
NCRR NIH HHS 1 S10 RR13866-01NCRR NIH HHS S10 RR013866NCRR NIH HHS S10 RR024601
6 · The paper itself

Abstract

Structural characterization of new α/γ-peptide foldamers containing the cyclically constrained γ-amino acid I is described. Crystallographic and 2D NMR analysis shows that γ residue I promotes the formation of a 12/10-helical secondary structure in α/γ-peptides. This helix contains two different types of internal H-bond, and the data show that the 12-atom C═O(i) → H-N(i+3) H-bond is more favorable than the 10-atom C═O(i) → H-N(i-1) H-bond. Several foldamer helices featuring topologically distinct H-bonds have been discovered, but our findings are the first to show that such H-bonds may differ in their favorability.

Indexed as

Hydrogen BondingPeptidesProtein Structure, SecondaryPeptides

Identifiers

PMID25974390
PMCPMC4687740

What OpenQuestion holds

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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.