Evidence map›Paper›PMID 31135160›Full record

ArticleThe journal of physical chemistry. B2019

4-Oxoproline as a Site-Specific Infrared Probe: Application To Assess Proline Isomerization and Dimer Formation.

Rachel M Abaskharon, Debopreeti Mukherjee, Feng Gai

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Rachel M AbaskharonDepartment of Chemistry , University of Pennsylvania , Philadelphia , Pennsylvania 19104 , United States.
Debopreeti MukherjeeDepartment of Chemistry , University of Pennsylvania , Philadelphia , Pennsylvania 19104 , United States.
Feng GaiDepartment of Chemistry , University of Pennsylvania , Philadelphia , Pennsylvania 19104 , United States.ORCID 0000-0003-1621-7119
University of Pennsylvania · US

Funding

Spectroscopic Study of Protein Folding DynamicsR01GM065978 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2002 to 2014
$3.9M
NIGMS NIH HHS R01 GM065978
6 · The paper itself

Abstract

Due to its unique structure, proline plays important structural and functional roles in proteins. However, this special amino acid lacks an adequate vibrational mode that can be exploited to probe its local electrostatic and hydration status via infrared spectroscopy. Herein, we show that the C═O stretching vibration of a proline derivative, 4-oxoproline, is sensitive to local environment and hence can be used as a site-specific infrared probe. We further validate this notion by applying this unnatural amino acid to assess the thermodynamics of proline cis-trans isomerization in a peptide environment and examine the amino acid dimer formation in concentrated proline and glycine solutions.

Indexed as

DimerizationIsomerismMolecular StructureProlineQuantum TheorySpectroscopy, Fourier Transform InfraredStatic ElectricityThermodynamicsWater4-ketoprolineProlineWater

Identifiers

PMID31135160
PMCPMC6599745
OpenAlexW2946925110

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.