Evidence map›Paper›PMID 29303586›Full record

ArticleThe journal of physical chemistry. B2018

Denaturants Alter the Flux through Multiple Pathways in the Folding of PDZ Domain.

Zhenxing Liu, D Thirumalai

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

2 authors.

Zhenxing LiuDepartment of Physics, Beijing Normal University , Beijing 100875, China.ORCID 0000-0001-9371-6929
D ThirumalaiDepartment of Chemistry, The University of Texas at Austin , Austin, Texas 78712, United States.ORCID 0000-0003-1801-5924

Funding

Computational Approaches to Single Molecule Force SpectroscopyR01GM089685 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI THIRUMALAI, DEVARAJAN · 2010 to 2020
$2.9M
NIGMS NIH HHS R01 GM089685
6 · The paper itself

Abstract

Although we understand many aspects of how small proteins (number of residues less than about hundred) fold, it is a major challenge to quantitatively describe how large proteins self-assemble. To partially overcome this challenge, we performed simulations using the self-organized polymer model with side chains (SOP-SC) in guanidinium chloride (GdmCl), using the molecular transfer model (MTM), to describe the folding of the 110-residue PDZ3 domain. The simulations reproduce the folding thermodynamics accurately including the melting temperature (T

Indexed as

GuanidineKineticsMolecular Dynamics SimulationPDZ DomainsProtein DenaturationProtein FoldingProteinsThermodynamicsGuanidineProteins

Identifiers

PMID29303586
PMCPMC5893999

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.