Evidence map›Paper›PMID 19919143›Full record

ArticleJournal of the American Chemical Society2009

Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching.

Jianhua Xu, Jiejin Chen, Dmitri Toptygin, Olga Tcherkasskaya, Patrik Callis, Jonathan King, Ludwig Brand, Jay R Knutson

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 45 citations in OpenAlex.

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  12. Upconversion spectrophotofluorometry.Methods in molecular biology (Clifton, N.J.) · 2014
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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

8 authors at 4 institutions in 1 country.

Jianhua XuOptical Spectroscopy Section, Laboratory of Molecular Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-1412, USA.
Jiejin Chen
Dmitri Toptygin
Olga Tcherkasskaya
Patrik Callis
Jonathan King
Ludwig Brand
Jay R Knutson
Johns Hopkins University · USMontana State University · USNational Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Time Resolved Fluorescence SpectroscopyZIAHL001452 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNUTSON, JAY R · 2009 to 2025
$5.1M
Folding &Misfolding of Parallel Beta-Helix ProteinsR01GM017980 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KING, JONATHAN ALAN · 1985 to 2009
$4.9M
Human gammaD-Crystallin Folding Misfolding &Fibril FormR01EY015834 · NEI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KING, JONATHAN ALAN · 2005 to 2014
$3.5M
PHOSPHOENOLPYRUVATE:GLYCOSE PHOSPHOTRANSFERASE SYSTEMR01GM038759 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROSEMAN, SAUL · 1987 to 2004
$3.0M
TIME RESOLVED FLUORESCENCE SPECTROSCOPYZ01HL001452 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNUTSON, JAY R · 1985 to 2008
$2.9M
BACTERIOPHAGE ASSEMBLY AND ITS GENETIC CONTROLR37GM017980 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KING, JONATHAN A · 1988 to 1997
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MECHANISM OF DNA REPLICATION IN XENOPUS EXTRACTSF32GM017980 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI WALTER, JOHANNES · 1995 to 1997
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PHOSPHOENOLPYRUVATE:GLYCOSE PHOSPHOTRANSFERASE SYSTEMR37GM038759 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROSEMAN, SAUL · 1987 to 1996
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Intramural NIH HHS Z01 HL001452NEI NIH HHS EY 015834NEI NIH HHS R01 EY015834NIGMS NIH HHS F32 GM017980NIGMS NIH HHS GM 17980NIGMS NIH HHS GM 38759NIGMS NIH HHS R01 GM017980NIGMS NIH HHS R01 GM038759
6 · The paper itself

Abstract

The eye lens Crystallin proteins are subject to UV irradiation throughout life, and the photochemistry of damage proceeds through the excited state; thus, their tryptophan (Trp) fluorescence lifetimes are physiologically important properties. The time-resolved fluorescence spectra of single Trps in human gammaD- and gammaS-Crystallins have been measured with both an upconversion spectrophotofluorometer on the 300 fs to 100 ps time scale, and a time correlated single photon counting apparatus on the 100 ps to 10 ns time scale, respectively. Three Trps in each wild type protein were replaced by phenylalanine, leading to single-Trp mutants: W68-only and W156-only of HgammaD- and W72-only and W162-only of HgammaS-Crystallin. These proteins exhibit similar ultrafast signatures: positive definite decay associated spectra (DAS) for 50-65 ps decay constants that indicate dominance of fast, heterogeneous quenching. The quenched population (judged by amplitude) of this DAS differs among mutants. Trps 68, 156 in human gammaD- and Trp72 in human gammaS-Crystallin are buried, but water can reach amide oxygen and ring HE1 atoms through narrow channels. QM-MM simulations of quenching by electron transfer predict heterogeneous decay times from 50-500 ps that agree with our experimental results. Further analysis of apparent radiative lifetimes allow us to deduce that substantial subpopulations of Trp are fully quenched in even faster (sub-300 fs) processes for several of the mutants. The quenching of Trp fluorescence of human gammaD- and gammaS-Crystallin may protect them from ambient light induced photo damage.

Indexed as

gamma-CrystallinsHumansPhenylalanineSpectrometry, FluorescenceTryptophanUltraviolet Raysgamma-CrystallinsPhenylalanineTryptophan

Identifiers

PMID19919143
PMCPMC3439204
OpenAlexW2003636651

What OpenQuestion holds

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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.