Evidence map›Paper›PMID 9083690›Full record

ArticleBiophysical journal1997

Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data.

E J Hustedt, A I Smirnov, C F Laub, C E Cobb, A H Beth

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 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
11.0field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 142 citations in OpenAlex.

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  17. The global analysis of DEER data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012
    Article
  18. Article
  19. What site-directed labeling studies tell us about the mechanism of rhodopsin activation and G-protein binding.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2010
    Review
  20. 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

5 authors at 1 institution in 1 country.

E J HustedtDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232, USA.
A I Smirnov
C F Laub
C E Cobb
A H Beth
Vanderbilt University · US

Funding

EPR STUDIES OF MEMBRANE PROTEINSR37HL034737 · NHLBI · VANDERBILT UNIVERSITY · PI BETH, ALBERT H · 1998 to 2007
$2.5M
MOLECULAR PHYSIOLOGY &BIOPHYSICSR01HL034737 · NHLBI · VANDERBILT UNIVERSITY · PI BETH, ALBERT H · 1985 to 1998
–
ELECTRON PARAMAGNETIC RESONANCE SPECTROMETERS10RR004075 · NCRR · VANDERBILT UNIVERSITY · PI BETH, ALBERT H · 1988 to 1988
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NCRR NIH HHS RR 01811NCRR NIH HHS RR 04075NHLBI NIH HHS HL 34737
6 · The paper itself

Abstract

For immobilized nitroxide spin-labels with a well-defined interprobe geometry, resolved dipolar splittings can be observed in continuous wave electron paramagnetic resonance (CW-EPR) spectra for interelectron distances as large as 30 A using perdeuterated probes. In this work, algorithms are developed for calculating CW-EPR spectra of immobilized, dipolar coupled nitroxides, and then used to define the limits of sensitivity to the interelectron distance as a function of geometry and microwave frequency. Secondly, the CW-EPR spectra of N epsilon-spin-labeled coenzyme NAD+ bound to microcrystalline, tetrameric glyceraldehyde-3-phosphate dehydrogenase (GAPDH) have been collected at 9.8, 34, and 94 GHz. These data have been analyzed, using a combination of simulated annealing and global analysis, to obtain a unique fit to the data. The values of the intermitroxide distance and the five angles defining the relative orientation of the two nitroxides are in reasonable agreement with a molecular model built from the known crystal structure. Finally, the effect of rigid body isotropic rotational diffusion on the CW-EPR spectra of dipolar coupled nitroxides has been investigated using an algorithm based on Brownian dynamics trajectories. These calculations demonstrate the sensitivity of CW-EPR spectra to dipolar coupling in the presence of rigid body rotational diffusion.

Indexed as

Electron Spin Resonance SpectroscopySpin LabelsAlgorithmsAnimalsDiffusionGlyceraldehyde-3-Phosphate DehydrogenasesMathematicsMolecular StructureMuscle, SkeletalNADProtein ConformationRabbitsGlyceraldehyde-3-Phosphate DehydrogenasesNADSpin Labels

Identifiers

PMID9083690
PMCPMC1184380
OpenAlexW1963687863

What OpenQuestion holds

Textmetadata
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.