Evidence map›Paper›PMID 32401513›Full record

ArticleThe journal of physical chemistry letters2020

Revealing the Dynamical Role of Co-solvents in the Coupled Folding and Dimerization of Insulin.

Xin-Xing Zhang, Andrei Tokmakoff

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 40% of its field
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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. 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 at 1 institution in 1 country.

Xin-Xing ZhangDepartment of Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, United States.ORCID http://orcid.org/0000-0001-6974-4727
Andrei TokmakoffDepartment of Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, United States.ORCID http://orcid.org/0000-0002-2434-8744
University of Chicago · US

Funding

The Dynamics of Molecular Recognition by Proteins from 2D IR Spectroscopy and MD SimulationsR01GM118774 · NIGMS · UNIVERSITY OF CHICAGO · PI TOKMAKOFF, ANDREI · 2016 to 2019
$1.6M
NIGMS NIH HHS R01 GM118774
6 · The paper itself

Abstract

Solvent-protein interactions are important for protein biological functions, especially for a coupled folding and binding system such as insulin. By monitoring the change in the conformation of insulin dimers during dissociation with temperature-jump infrared spectroscopy, we show that co-solvents can significantly destabilize the dimers by perturbing their hydrophobic center. The transition from the native to intermediate dimer state is observed as the buried residues are exposed to solvents in the presence of 10% dimethyl sulfoxide and with α-helices unfolding when ethanol is present, which reduces the dissociation time dramatically to 50% and 20% of the value in a D

Indexed as

DimerizationDimethyl SulfoxideEthanolInsulinProtein ConformationSolventsDimethyl SulfoxideEthanolInsulininsulin dimersSolvents

Identifiers

PMID32401513
PMCPMC7850624
OpenAlexW3024340559

What OpenQuestion holds

Textmetadata
LicenceTDM
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.