Evidence map›Paper›PMID 36573077›Full record

ArticleACS measurement science au2022

Measuring the Radius of Gyration and Intrinsic Flexibility of Viral Proteins in Buffer Solution Using Small-Angle X-ray Scattering.

Riccardo Funari, Nikhil Bhalla, Luigi Gentile

Open access · goldAbstract read
In one paragraph

Article in ACS measurement science au, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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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

3 authors at 3 institutions in 2 countries.

Riccardo FunariDepartment of Physics "M. Merlin", University of Bari Aldo Moro, Via Amendola, 173, Bari 70125, Italy.ORCID https://orcid.org/0000-0003-1786-3833
Nikhil BhallaNanotechnology and Integrated Bioengineering Centre (NIBEC), School of Engineering, Ulster University, Jordanstown, Shore Road, Northern Ireland BT37 0QB, United Kingdom.ORCID https://orcid.org/0000-0002-4720-3679
Luigi GentileDepartment of Chemistry, University of Bari Aldo Moro, Edoardo Orabona 4, Bari 70125, Italy.ORCID https://orcid.org/0000-0001-6854-2963
Center for Biomolecular Nanotechnologies · ITConsorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase · ITUniversity of Ulster · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Measuring structural features of proteins dispersed in buffer solution, in contrast to crystal form, is indispensable in understanding morphological characteristics of the biomolecule in a native environment. We report on the structure and apparent viscosity of unfolded α and β variants of SARS-CoV-2 spike proteins dispersed in buffer solutions. The radius of gyration of the β variant is found to be larger than that of the α variant, while the ab initio computation of one of the possible particle-like bodies is consistent with the small-angle X-ray scattering (SAXS) profiles resembling a conformation similar to the three-dimensional structure of the folded state of the corresponding α and β spike variant. However, a smaller radius of gyration with respect to the predicted folded state of 2.4 and 2.7 is observed for both α and β variants, respectively. Our work complements the structural characterization of spike proteins using cryo-electron microscopy techniques. The measurement/analysis discussed here might be useful for quick and cost-effective evaluation of several protein structures, let alone mutated viral proteins, which is useful for drug discovery/development applications.

Identifiers

PMID36573077
PMCPMC9783065
OpenAlexW4296579788

What OpenQuestion holds

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LicenceCC BY
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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.