Evidence map›Paper›PMID 27447848›Full record

ArticleThe journal of physical chemistry letters2016

Fluorescence from Multiple Chromophore Hydrogen-Bonding States in the Far-Red Protein TagRFP675.

Patrick E Konold, Eunjin Yoon, Junghwa Lee, Samantha L Allen, Prem P Chapagain, Bernard S Gerstman, Chola K Regmi, Kiryl D Piatkevich, Vladislav V Verkhusha, Taiha Joo and 1 more

Open access · greenAbstract readLetter
PubMed Full text at PMC Publisher
In one paragraph

Article in The journal of physical chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 13% of its field
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

3 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

11 authors at 7 institutions in 2 countries.

Patrick E KonoldJILA, University of Colorado and NIST , Boulder, Colorado 80309, United States.
Eunjin YoonDepartment of Chemistry, Pohang University of Science and Technology (POSTECH) , Pohang, South Korea 790-784.
Junghwa LeeDepartment of Chemistry, Pohang University of Science and Technology (POSTECH) , Pohang, South Korea 790-784.
Samantha L AllenJILA, University of Colorado and NIST , Boulder, Colorado 80309, United States.
Prem P ChapagainDepartment of Physics, Florida International University , Miami, Florida 33199, United States.
Bernard S GerstmanDepartment of Physics, Florida International University , Miami, Florida 33199, United States.
Chola K RegmiDepartment of Physics, Florida International University , Miami, Florida 33199, United States.
Kiryl D PiatkevichMassachusetts Institute of Technology Media Lab, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Vladislav V VerkhushaDepartment of Anatomy & Structural Biology, Albert Einstein College of Medicine , Bronx, New York 10461, United States.
Taiha JooDepartment of Chemistry, Pohang University of Science and Technology (POSTECH) , Pohang, South Korea 790-784.
Ralph JimenezJILA, University of Colorado and NIST , Boulder, Colorado 80309, United States.
Pohang University of Science and Technology · KRFlorida International University · USUniversity of Colorado Boulder · USAlbert Einstein College of Medicine · USJoint Institute for Laboratory Astrophysics · USMassachusetts Institute of Technology · USVirginia Tech · US

Funding

Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
Technologies to Define and Map Novel Interorganelle Macromolecular InteractionsR01GM105997 · NIGMS · UNIVERSITY OF COLORADO · PI AHN, NATALIE G., PALMER, AMY E · 2013 to 2016
$1.6M
Engineering bacterial phytochromes for near-infrared imaging in mammalsR01GM108579 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2014 to 2017
$1.3M
Computational Investigations of Monomeric Variants of Red Fluorescent ProteinsSC3GM096903 · NIGMS · FLORIDA INTERNATIONAL UNIVERSITY · PI CHAPAGAIN, PREM P · 2011 to 2014
$425k
NIGMS NIH HHS R01 GM105997NIGMS NIH HHS R01 GM108579NIGMS NIH HHS SC3 GM096903NIGMS NIH HHS T32 GM065103
6 · The paper itself

Abstract

Far-red fluorescent proteins are critical for in vivo imaging applications, but the relative importance of structure versus dynamics in generating large Stokes-shifted emission is unclear. The unusually red-shifted emission of TagRFP675, a derivative of mKate, has been attributed to the multiple hydrogen bonds with the chromophore N-acylimine carbonyl. We characterized TagRFP675 and point mutants designed to perturb these hydrogen bonds with spectrally resolved transient grating and time-resolved fluorescence (TRF) spectroscopies supported by molecular dynamics simulations. TRF results for TagRFP675 and the mKate/M41Q variant show picosecond time scale red-shifts followed by nanosecond time blue-shifts. Global analysis of the TRF spectra reveals spectrally distinct emitting states that do not interconvert during the S1 lifetime. These dynamics originate from photoexcitation of a mixed ground-state population of acylimine hydrogen bond conformers. Strategically tuning the chromophore environment in TagRFP675 might stabilize the most red-shifted conformation and result in a variant with a larger Stokes shift.

Indexed as

FluorescenceHydrogen BondingLuminescent ProteinsMolecular ConformationMolecular Dynamics SimulationRed Fluorescent ProteinLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID27447848
PMCPMC5004773
OpenAlexW2483626464

What OpenQuestion holds

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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.