Evidence map›Paper›PMID 25215518›Full record

ArticleThe journal of physical chemistry. B2014

Experimental validation of the role of trifluoroethanol as a nanocrowder.

Robert M Culik, Rachel M Abaskharon, Ileana M Pazos, Feng Gai

Open access · bronzeAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Deciphering the Mechanistic Basis for Perfluoroalkyl-Protein Interactions.Chembiochem : a European journal of chemical biology · 2023
    Article
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  10. Helical Structure of Recombinant Melittin.The journal of physical chemistry. B · 2019
    Article
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  12. Article
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  14. 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

4 authors at 1 institution in 1 country.

Robert M CulikDepartment of Biochemistry & Biophysics and ‡Department of Chemistry, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
Rachel M Abaskharon
Ileana M Pazos
Feng Gai
University of Pennsylvania · US

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Spectroscopic Study of Protein Folding DynamicsR01GM065978 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2002 to 2014
$3.9M
NIGMS NIH HHS GM-008275NIGMS NIH HHS GM-065978NIGMS NIH HHS R01 GM065978NIGMS NIH HHS T32 GM008275NIGMS NIH HHS T32-GM008275
6 · The paper itself

Abstract

Trifluoroethanol (TFE) is commonly used to induce protein secondary structure, especially α-helix formation. Due to its amphiphilic nature, however, TFE can also self-associate to form micellelike, nanometer-sized clusters. Herein, we hypothesize that such clusters can act as nanocrowders to increase protein folding rates via the excluded volume effect. To test this hypothesis, we measure the conformational relaxation kinetics of an intrinsically disordered protein, the phosphorylated kinase inducible domain (pKID), which forms a helix-turn-helix in TFE solutions. We find that the conformational relaxation rate of pKID displays a rather complex dependence on TFE percentage (v/v): while it first decreases between 0 and 5%, between 5 and 15% the rate increases and then remains relatively unchanged between 15 and 30% and finally decreases again at higher percentages (i.e., 50%). This trend coincides with the fact that TFE clustering is maximized in the range of 15-30%, thus providing validation of our hypothesis. Another line of supporting evidence comes from the observation that the relaxation rate of a monomeric helical peptide, which due to its predominantly local interactions in the folded state is less affected by crowding, does not show a similar TFE dependence.

Indexed as

Amino Acid SequenceCircular DichroismMolecular Sequence DataPeptidesPhosphorylationProtein FoldingProtein Structure, SecondaryProtein UnfoldingTemperatureThermodynamicsTrifluoroethanolPeptidesTrifluoroethanol

Identifiers

PMID25215518
PMCPMC4183368
OpenAlexW2331392892

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.