Evidence map›Paper›PMID 40376407›Full record

ReviewBiophysical reviews2025

Protein folding: basic statistical physics models and computational multipopulation genetic algorithms.

Luis Olivares-Quiroz, Marcos Angel Gonzalez Olvera

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2025. 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

2 authors.

Luis Olivares-QuirozAcademia de Física y Posgrado en Ciencias de la Complejidad, Universidad Autónoma de la Ciudad de México, Prol. San Isidro 151, San Lorenzo Tezonco, Iztapalapa, Ciudad de Mexico, 09790 CDMX Mexico.
Marcos Angel Gonzalez Olvera *Colegio de Ciencia y Tecnología, Universidad Autónoma de la Ciudad de México, Prol. San Isidro 151, San Lorenzo Tezonco, Iztapalapa, Mexico City, 09790 CDMX Mexico.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work, we present a brief and concise review about the main features of protein folding which is one of the central research questions at the interface of physics, molecular biology, and computational sciences. We describe the physical foundations of the protein folding phenomenon itself and how it arises as both a free energy minimization process combined with a hydrophobic collapse of the enzyme molten globule due to inter and intramolecular forces among amino acid residues themselves and water molecules. We cover briefly some basic statistical physics-based models to predict the thermodynamic properties of the protein folding transition. Then, we focus our attention on the implementation of computational algorithms designed to minimize energy functions in polypeptides.

Indexed as

Energy minimizationGenetic algorithmsHydrophobic collapseProtein foldingStatistical physics

Identifiers

PMID40376407
PMCPMC12075078

What OpenQuestion holds

Textmetadata
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.