Evidence map›Paper›PMID 25716887›Full record

ArticlePhysical chemistry chemical physics : PCCP2015

p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore-quencher pair for short distance measurements: application to polyproline peptides.

Mary Rose Mintzer, Thomas Troxler, Feng Gai

Abstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Site-Specific Interrogation of Protein Structure and Stability.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  3. Article
  4. Article
  5. Minimalist IR and fluorescence probes of protein function.Current opinion in chemical biology · 2016
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. 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

3 authors.

Mary Rose MintzerDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
Thomas Troxler
Feng Gai

Funding

ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
Spectroscopic Study of Protein Folding DynamicsR01GM065978 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2002 to 2014
$3.9M
NIGMS NIH HHS GM-065978NIGMS NIH HHS P41 GM104605NIGMS NIH HHS P41-GM104605NIGMS NIH HHS R01 GM065978
6 · The paper itself

Abstract

The C≡N stretching frequency and fluorescence quantum yield of p-cyanophenylalanine are sensitive to environment. As such, this unnatural amino acid has found broad applications, ranging from studying how proteins fold to determining the local electric field of membranes. Herein, we demonstrate that the fluorescence of p-cyanophenylalanine can be quenched by selenomethionine through an electron transfer process occurring at short distances, thus further expanding its spectroscopic utility. Using this fluorophore-quencher pair, we are able to show that short polyproline peptides (1-4 prolines) are not rigid; instead, they sample a bimodal conformational distribution.

Indexed as

AlanineFluorescent DyesKineticsMolecular Dynamics SimulationNitrilesPeptidesPhenylalanineProtein ConformationSelenomethionineSpectrometry, FluorescenceAlanineFluorescent DyesNitrilesp-cyanophenylalaninePeptidesPhenylalaninepolyprolineSelenomethionine

Identifiers

PMID25716887
PMCPMC4357573

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.