Evidence map›Paper›PMID 39119519›Full record

ArticleFrontiers in chemistry2024

Water determines the intramolecular dynamics of proteins. En example of bovine serum albumin.

Nikita V Penkov

Abstract read
In one paragraph

Article in Frontiers in chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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

2 citing papers in PubMed.

  1. Primary biomolecular adsorption energetics of core-shell nanocomplexes: Implications for biological interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Advances in Terahertz Biophysics and Chemistry.Research (Washington, D.C.) · 2025
    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

1 author.

Nikita V PenkovInstitute of Cell Biophysics, Federal Research Center "Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences", Pushchino, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work, the terahertz time-domain spectroscopy method analyzed solutions of bovine serum albumin (BSA) in two high concentrations (50 and 334 mg/mL) at three pH values (2.5, 6.5, 8.5) and the same solvents without protein, at 25°C. The spectra of dry BSA were also recorded. For the first time, a method for determining the complex dielectric permittivity of protein molecules in aqueous solutions, without the dielectric contribution of the aqueous phase, is proposed. It is shown that the dielectric permittivity of dissolved and dry BSA (lyophilized, in the native conformation) differ significantly in the terahertz frequency range. These differences are small near 70 cm

Indexed as

BSAdielectric spectrahydrate shellsnative conformationprotein dynamicsTHzTHz-TDS

Identifiers

PMID39119519
PMCPMC11306983

What OpenQuestion holds

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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.