Evidence map›Paper›PMID 20225890›Full record

ArticleBiochemistry2010

Circular dichroism and UV resonance raman study of the impact of alcohols on the Gibbs free energy landscape of an alpha-helical peptide.

Kan Xiong, Sanford A Asher

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 22 citations in OpenAlex.

  1. Biomolecular Condensates Dictate the Folding Landscape of Proteins.bioRxiv : the preprint server for biology · 2026
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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.

Kan XiongDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Sanford A Asher
University of Pittsburgh · US

Funding

University of Pittsburgh Clinical and Translational Science InstituteUL1TR000005 · NCATS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI REIS, STEVEN E · 2012 to 2015
$50.8M
UV Resonance Raman Studies of Protein StructureR01EB002053 · NIBIB · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ASHER, SANFORD A. · 2003 to 2008
$2.1M
Ultrahigh Throughput Deep UV Raman Spectrometer for Probing Protein StructureR01EB009089 · NIBIB · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ASHER, SANFORD A. · 2008 to 2011
$1.3M
NCATS NIH HHS UL1 TR000005NIBIB NIH HHS 1R01EB009089NIBIB NIH HHS GM8RO1EB002053NIBIB NIH HHS R01 EB002053NIBIB NIH HHS R01 EB009089
6 · The paper itself

Abstract

We used CD and UV resonance Raman spectroscopy to study the impact of alcohols on the conformational equilibria and relative Gibbs free energy landscapes along the Ramachandran Psi-coordinate of a mainly poly-Ala peptide, AP with an AAAAA(AAARA)(3)A sequence. 2,2,2-Trifluoroethanol (TFE) most stabilizes the alpha-helix-like conformations, followed by ethanol, methanol, and pure water. The pi-bulge conformation is stabilized more than the alpha-helix, while the 3(10)-helix is destabilized due to the alcohol-increased hydrophobicity. Turns are also stabilized by alcohols. We also found that while TFE induces more alpha-helices, it favors multiple, shorter helix segments.

Indexed as

AlcoholsAmino Acid SequenceCircular DichroismEthanolIndicators and ReagentsMethanolModels, MolecularPeptidesProtein ConformationSpectrophotometry, UltravioletSpectrum Analysis, RamanThermodynamicsWaterAlcoholsEthanolIndicators and ReagentsMethanolPeptidesWater

Identifiers

PMID20225890
PMCPMC2857330
OpenAlexW2007089204

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.