Evidence map›Paper›PMID 41759065›Full record

ArticleThe journal of physical chemistry. B2026

Quantitative Integration of FRET and Molecular Dynamics for Modeling Flexible Peptides.

Danilo Roccatano

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Danilo RoccatanoSchool of Engineering and Physical Sciences, University of Lincoln, Brayford Pool, Lincoln LN6 7TS, U.K.ORCID 0000-0002-8495-3815

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flexible protein regions, often enriched in glycine- and serine-rich segments, play a central role in biomolecular dynamics and function. The combination of time-resolved fluorescence resonance energy transfer (FRET) spectroscopy and molecular dynamics simulations provides a powerful framework to characterize these motions at atomic resolution. In this work, we investigate the conformational and kinetic properties of Trp-(GS)

Indexed as

Fluorescence Resonance Energy TransferMolecular Dynamics SimulationPeptidesKineticsProtein ConformationPeptides

Identifiers

PMID41759065
PMCPMC12990115

What OpenQuestion holds

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LicenceCC BY
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.