Evidence map›Paper›PMID 9251821›Full record

ArticleBiophysical journal1997

Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C.

M She, W J Dong, P K Umeda, H C Cheung

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

7 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Nucleotide activation of the Ca-ATPase.The Journal of biological chemistry · 2012
    Article
  4. Article
  5. Article
  6. Article
  7. On spectral relaxation in proteins.Photochemistry and photobiology · 2000
    Review
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

4 authors at 1 institution in 1 country.

M SheDepartment of Physics, University of Alabama at Birmingham 35294, USA.
W J Dong
P K Umeda
H C Cheung
University of Alabama at Birmingham · US

Funding

REGULATORY MECHANISMS OF CARDIAC MUSCLER01HL052508 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHEUNG, HERBERT C · 1996 to 2008
$2.6M
STUDIES ON MUSCLE REGULATORY PROTEINSR01AR025193 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CHEUNG, HERBERT C · 1986 to 1991
–
MOLECULAR DETERMINANTS OF GENE EXPRESSION IN THE HEARTR01HL044094 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI UMEDA, PATRICK · 1990 to 1994
–
NHLBI NIH HHS HL44094NHLBI NIH HHS HL52508NIAMS NIH HHS AR25193
6 · The paper itself

Abstract

The regulatory domain of troponin C (TnC) from chicken skeletal muscle was studied using genetically generated mutants which contained a single tryptophan at positions 22, 52, and 90. The quantum yields of Trp-22 are 0.33 and 0.25 in the presence of Mg2+ (2-Mg state) and Ca2+ (4-Ca state), respectively. The large quantum yield of the 2-Mg state is due to a relatively small nonradiative decay rate and consistent with the emission peak at 331 nm. The intensity decay of this state is monoexponential with a single lifetime of 5.65 ns, independent of wavelength. In the 4-Ca state, the decay is biexponential with the mean of the two lifetimes increasing from 4.54 to 4.92 ns across the emission band. The decay-associated spectrum of the short lifetime is red-shifted by 19 nm relative to the steady-state spectrum. The decay of Trp-52 is biexponential in the 2-Mg state and triexponential in the 4-Ca state. The decay of Trp-90 requires three exponential terms for a satisfactory fit, but can be fitted with two exponential terms in the 4-Ca state. The lower quantum yields (< 0.15) of these two tryptophans are due to a combination of smaller radiative and larger nonradiative decay rates. The results from Trp-22 suggest a homogeneous ground-state indole ring in the absence of bound Ca2+ at the regulatory sites and a ground-state heterogeneity induced by activator Ca2+. The Ca(2+)-induced environmental changes of Trp-52 and Trp-90 deviate from those predicted by a modeled structure of the 4-Ca state. The anisotropy decays of all three tryptophans show two rotational correlation times. The long correlation times (phi 1 = 8.1-8.3 ns) derived from Trp-22 and Trp-90 suggest an asymmetric hydrodynamic shape. TnC becomes more asymmetric upon binding activator Ca2+ (phi 1 = 10.1-11.6 ns). The values of phi 1 obtained from Trp-52 are 3-4 ns shorter than those from Trp-22 and Trp-90, and these reduced correlation times may be related to the mobility of the residue and/or local segmental flexibility.

Indexed as

Protein ConformationTryptophanAcrylamideAcrylamidesAnimalsCalciumChickensCloning, MolecularCrystallography, X-RayFluorescence PolarizationKineticsMagnesiumModels, MolecularMuscle Fibers, Fast-TwitchMuscle, SkeletalMutagenesis, Site-DirectedAcrylamideAcrylamidesCalciumMagnesiumRecombinant ProteinsTroponin CTryptophan

Identifiers

PMID9251821
PMCPMC1181001
OpenAlexW1983470205

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Registered trials

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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.