Evidence map›Paper›PMID 33800175›Full record

ArticleInternational journal of molecular sciences2021

Unfolding and Aggregation of Lysozyme under the Combined Action of Dithiothreitol and Guanidine Hydrochloride: Optical Studies.

Ruslan M Sarimov, Vladimir N Binhi, Tatiana A Matveeva, Nikita V Penkov, Sergey V Gudkov

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. pH-Dependent HEWL-AuNPs Interactions: Optical Study.Molecules (Basel, Switzerland) · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Molecular Dynamics-From Macromolecule to Small Molecules.International journal of molecular sciences · 2022
    Article
  10. Article
  11. 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 2 institutions in 1 country.

Ruslan M SarimovProkhorov General Physics Institute of the Russian Academy of Sciences, Vavilov St., 38, 119991 Moscow, Russia.ORCID 0000-0002-2751-1615
Vladimir N BinhiProkhorov General Physics Institute of the Russian Academy of Sciences, Vavilov St., 38, 119991 Moscow, Russia.
Tatiana A MatveevaProkhorov General Physics Institute of the Russian Academy of Sciences, Vavilov St., 38, 119991 Moscow, Russia.
Nikita V PenkovInstitute of Cell Biophysics of the Russian Academy of Sciences, PSCBR RAS, Institutskaya St., 3, Pushchino, 142290 Moscow, Russia.ORCID 0000-0003-2212-5640
Sergey V GudkovProkhorov General Physics Institute of the Russian Academy of Sciences, Vavilov St., 38, 119991 Moscow, Russia.ORCID 0000-0002-8814-6906
Prokhorov General Physics Institute · RUInstitute of Cell Biophysics · RU

Funding

Ministry of Science and Higher Education of the Russian Federation 075-15-2020-912
6 · The paper itself

Abstract

Using a number of optical techniques (interferometry, dynamic light scattering, and spectroscopy), denaturation of hen egg white lysozyme (HEWL) by treatment with a combination of dithiothreitol (DTT) and guanidine hydrochloride (GdnHCl) has been investigated. The denaturing solutions were selected so that protein denaturation occurred with aggregation (Tris-HCl pH = 8.0, 50 mM, DTT 30 mM) or without aggregation (Tris-HCl pH = 8.0, 50 mM, DTT 30 mM, GdnHCl 6 M) and can be evaluated after 60 min of treatment. It has been found that denatured by solution with 6 M GdnHCl lysozyme completely loses its enzymatic activity after 30 min and the size of the protein molecule increases by 1.5 times, from 3.8 nm to 5.7 nm. Denaturation without of GdnHCl led to aggregation with preserving about 50% of its enzymatic activity. Denaturation of HEWL was examined using interferometry. Previously, it has been shown that protein denaturation that occurs without subsequent aggregation leads to an increase in the refractive index (Δ

Indexed as

ChickensProtein AggregatesProtein UnfoldingAnimalsDithiothreitolGuanidineMuramidaseSpectrophotometry, UltravioletDithiothreitolGuanidineMuramidaseProtein Aggregatesanalysis of protein activitydynamic light scattering (DLS)interferometryoptical methods in biochemistryprotein hydration shellsUV/visible absorbance spectroscopy

Identifiers

PMID33800175
PMCPMC7962454
OpenAlexW3134297621

What OpenQuestion holds

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Read underepoch 390

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.