Evidence map›Paper›PMID 29892029›Full record

ArticleNature chemistry2018

Infrared spectroscopy reveals multi-step multi-timescale photoactivation in the photoconvertible protein archetype dronpa.

Sergey P Laptenok, Agnieszka A Gil, Christopher R Hall, Andras Lukacs, James N Iuliano, Garth A Jones, Gregory M Greetham, Paul Donaldson, Atsushi Miyawaki, Peter J Tonge and 1 more

Abstract read
In one paragraph

Article in Nature chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 64 citations in OpenAlex.

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  16. Photoswitchable Fluorescent Proteins: Mechanisms on Ultrafast Timescales.International journal of molecular sciences · 2022
    Review
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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 6 institutions in 6 countries.

Sergey P LaptenokSchool of Chemistry, University of East Anglia, Norwich, UK.ORCID http://orcid.org/0000-0002-6468-3010
Agnieszka A GilDepartment of Chemistry, Stony Brook University, Stony Brook, NY, USA.
Christopher R HallSchool of Chemistry, University of East Anglia, Norwich, UK.
Andras LukacsDepartment of Biophysics, Medical School, University of Pecs, Pecs, Hungary.
James N IulianoDepartment of Chemistry, Stony Brook University, Stony Brook, NY, USA.ORCID http://orcid.org/0000-0003-1213-3292
Garth A JonesSchool of Chemistry, University of East Anglia, Norwich, UK.
Gregory M GreethamCentral Laser Facility, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK.
Paul DonaldsonCentral Laser Facility, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK.
Atsushi MiyawakiLaboratory for Cell Function Dynamics, RIKEN Center for Brain Science, Wako, Saitama, Japan.
Peter J TongeDepartment of Chemistry, Stony Brook University, Stony Brook, NY, USA. peter.tonge@stonybrook.edu.ORCID http://orcid.org/0000-0003-1606-3471
Stephen R MeechSchool of Chemistry, University of East Anglia, Norwich, UK. s.meech@uea.ac.uk.ORCID http://orcid.org/0000-0001-5561-2782
University of East Anglia · GBResearch Complex at Harwell · GBStony Brook University · USPrinceton University · USRIKEN Center for Brain Science · JPUniversity of Pecs · HU

Funding

SBU Chemistry-Biology Interface Training ProgramT32GM092714 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI SAMPSON, NICOLE S, TONGE, PETER J · 2010 to 2019
$1.7M
NIGMS NIH HHS T32 GM092714
6 · The paper itself

Abstract

Photochromic fluorescent proteins play key roles in super-resolution microscopy and optogenetics. The light-driven structural changes that modulate the fluorescence involve both trans-to-cis isomerization and proton transfer. The mechanism, timescale and relative contribution of chromophore and protein dynamics are currently not well understood. Here, the mechanism of off-to-on-state switching in dronpa is studied using femtosecond-to-millisecond time-resolved infrared spectroscopy and isotope labelling. Chromophore and protein dynamics are shown to occur on multiple timescales, from picoseconds to hundreds of microseconds. Following excitation of the trans chromophore, a ground-state primary product is formed within picoseconds. Surprisingly, the characteristic vibrational spectrum of the neutral cis isomer appears only after several tens of nanoseconds. Further fluctuations in protein structure around the neutral cis chromophore are required to form a new intermediate, which promotes the final proton-transfer reaction. These data illustrate the interplay between chromophore dynamics and the protein environment underlying fluorescent protein photochromism.

Indexed as

Spectrophotometry, InfraredLuminescent ProteinsPhotochemical ProcessesProtein ConformationProtonsLuminescent ProteinsProtons

Identifiers

PMID29892029
PMCPMC6250569
OpenAlexW2801401091

What OpenQuestion holds

Textmetadata
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.