Evidence map›Paper›PMID 39337648›Full record

ArticleInternational journal of molecular sciences2024

Mechanical Properties of a Solvated Biomolecule: RGD (1FUV) Peptide.

Puja Adhikari, Bahaa Jawad, Wai-Yim Ching

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. 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

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

1 citing paper in PubMed.

  1. 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

3 authors.

Puja AdhikariDepartment of Physics and Astronomy, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Bahaa JawadDepartment of Physics and Astronomy, University of Missouri-Kansas City, Kansas City, MO 64110, USA.ORCID 0000-0001-6252-3999
Wai-Yim ChingDepartment of Physics and Astronomy, University of Missouri-Kansas City, Kansas City, MO 64110, USA.ORCID 0000-0001-7738-8822

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanical properties of proteins/peptides play an essential role in their functionalities and implications, as well as their structure and dynamic properties. Understanding mechanical properties is pivotal to our knowledge of protein folding and the molecular basis of diverse cellular processes. Herein, we present a computational approach using ab initio quantum mechanical calculations to determine the mechanical properties-such as bulk modulus, shear modulus, Young's modulus, and Poisson's ratio-of a solvated Arg-Gly-Asp (RGD) peptide model. Since this peptide serves as the RGD-directed integrin recognition site and may participate in cellular adhesion, it is considered a promising small peptide for medicinal applications. This successful approach paves the way for investigating larger and more complex biomolecules.

Indexed as

OligopeptidesElastic ModulusModels, MolecularPeptidesQuantum Theoryarginyl-glycyl-aspartic acidOligopeptidesPeptidesdensity functional theorymechanical propertiesRGD peptidesolvated biomolecule

Identifiers

PMID39337648
PMCPMC11432424

What OpenQuestion holds

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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.