Evidence map›Paper›PMID 40560561›Full record

ArticleThe journal of physical chemistry. B2025

Validation of the "Stoichiometric Hydration Ice-Bridge Model" Provides Method To Predict Protein Folding Energetics.

Gary D Fullerton, Andres Rahal

Abstract readValidation Study
In one paragraph

Article in The journal of physical chemistry. B, 2025. 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

2 authors.

Gary D FullertonDepartment of Radiology, University of Texas Health SA, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900, United States.ORCID 0009-0006-9621-4987
Andres RahalDepartment of Radiology, University of Texas Health SA, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hydration of macromolecules plays a critical role in powering functional macromolecular shape changes to open/close cellular pores, clip protein chains, and perform a myriad of other functions critical to life. This study of collagen "bound water" offers insight into these processes by quantifying protein hydration energetics powered by ice-bridge formation on protein backbones. Quantification of ice-bridge properties on rat tail tendon is uniquely possible because the elevated stability of mammalian collagen at laboratory temperature provides 100% at-rest in vitro occupancy of backbone tripeptide units serving as ice nucleation sites. Full occupancy

Indexed as

CollagenIceProtein FoldingWaterAnimalsRatsThermodynamicsCollagenIceWater

Identifiers

PMID40560561
PMCPMC12235632

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.