How Useful can the Voigt Profile be in Protein Folding Processes?

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Article in The protein journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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

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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

1 citing paper in PubMed.

Raman Spectroscopy Reveals Photobiomodulation-Induced α-Helix to β-Sheet Transition in Tubulins: Potential Implications for Alzheimer's and Other Neurodegenerative Diseases.Nanomaterials (Basel, Switzerland) · 2024
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

2 authors.

Luka MaisuradzeDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520-8114, USA.

Gia G MaisuradzeBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, 14853-1301, USA. gm56@cornell.edu.ORCID 0000-0002-1901-8433

Funding

INTERNAL BONDIN IN PROTEINSR01GM014312 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MAISURADZE, GIA, RACKOVSKY, SHALOM R · 1985 to 2021

$9.4M

NIGMS NIH HHS R01 GM014312NIH HHS GM-14312

6 · The paper itself

Abstract

The analytical expression for the Voigt profile, along with its simplified forms for the Gaussian and Lorentzian dominance, is presented. The applicability of the Voigt profile in the description of anomalous diffusion phenomena, ubiquitous in different fields of science including protein folding, is discussed. It is shown that the Voigt profile is a good descriptor of the processes occurring in protein folding and in the native state. The usefulness of the Voigt profile in deriving important information of the diffusive motions in proteins from a quasielastic incoherent neutron scattering experiments is illustrated.

Indexed as

Models, ChemicalModels, StatisticalProtein FoldingProteinsMolecular Dynamics SimulationProteinsGaussian and lorentzian functionsLevy flightMolecular dynamics simulationsProtein foldingQuasielastic neutron-scattering spectraVoigt profile

Identifiers

PMID33398661

DOI10.1007/s10930-020-09954-5

PMCPMC8026557

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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.