Evidence map›Paper›PMID 31101718›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy.

Toru Kondo, Jesse B Gordon, Alberta Pinnola, Luca Dall'Osto, Roberto Bassi, Gabriela S Schlau-Cohen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. LHCSR1 Functions as a Dimmer Switch for Light Harvesting.The journal of physical chemistry letters · 2026
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  3. Evidence of a Three-State Mechanism in DNA Hairpin Folding.Journal of the American Chemical Society · 2025
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  19. Single-molecule FRET methods to study the dynamics of proteins at work.Current opinion in biomedical engineering · 2019
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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

6 authors at 2 institutions in 2 countries.

Toru KondoDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139; tkondo@mit.edu gssc@mit.edu.
Jesse B GordonDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139.
Alberta PinnolaDepartment of Biotechnology, University of Verona, 37134 Verona, Italy.ORCID 0000-0001-8373-7638
Luca Dall'OstoDepartment of Biotechnology, University of Verona, 37134 Verona, Italy.
Roberto BassiDepartment of Biotechnology, University of Verona, 37134 Verona, Italy.ORCID 0000-0002-4140-8446
Gabriela S Schlau-CohenDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139; tkondo@mit.edu gssc@mit.edu.ORCID 0000-0001-7746-2981
Massachusetts Institute of Technology · USUniversity of Verona · IT

Funding

Wide-Field Short-Wave Infrared (SWIR) multiphoton (MP) tissue imagingP41EB015871 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SO, PETER T. · 2012 to 2021
$11.3M
NIBIB NIH HHS P41 EB015871
6 · The paper itself

Abstract

Biological systems are subjected to continuous environmental fluctuations, and therefore, flexibility in the structure and function of their protein building blocks is essential for survival. Protein dynamics are often local conformational changes, which allows multiple dynamical processes to occur simultaneously and rapidly in individual proteins. Experiments often average over these dynamics and their multiplicity, preventing identification of the molecular origin and impact on biological function. Green plants survive under high light by quenching excess energy, and Light-Harvesting Complex Stress Related 1 (LHCSR1) is the protein responsible for quenching in moss. Here, we expand an analysis of the correlation function of the fluorescence lifetime by improving the estimation of the lifetime states and by developing a multicomponent model correlation function, and we apply this analysis at the single-molecule level. Through these advances, we resolve previously hidden rapid dynamics, including multiple parallel processes. By applying this technique to LHCSR1, we identify and quantitate parallel dynamics on hundreds of microseconds and tens of milliseconds timescales, likely at two quenching sites within the protein. These sites are individually controlled in response to fluctuations in sunlight, which provides robust regulation of the light-harvesting machinery. Considering our results in combination with previous structural, spectroscopic, and computational data, we propose specific pigments that serve as the quenching sites. These findings, therefore, provide a mechanistic basis for quenching, illustrating the ability of this method to uncover protein function.

Indexed as

FluorescenceLightLight-Harvesting Protein ComplexesPhotosynthesisSingle Molecule ImagingLight-Harvesting Protein Complexesnonphotochemical quenchingphotosynthetic light harvestingprotein dynamicssingle-molecule fluorescence spectroscopy

Identifiers

PMID31101718
PMCPMC6561297
OpenAlexW2945562222

What OpenQuestion holds

Textmetadata
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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.