Evidence map›Paper›PMID 31475422›Full record

ArticleChembiochem : a European journal of chemical biology2020

Compactness of Protein Folds Alters Disulfide-Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins.

Dániel Horváth, Nóra Taricska, Ernő Keszei, Pál Stráner, Viktor Farkas, Gábor K Tóth, András Perczel

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Article in Chembiochem : a European journal of chemical biology, 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
–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

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
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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

7 authors.

Dániel HorváthLaboratory of Structural Chemistry and Biology and, MTA-ELTE Protein Modeling Research Group at the Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, 1518, Budapest, Hungary.ORCID 0000-0001-8239-3933
Nóra TaricskaLaboratory of Structural Chemistry and Biology and, MTA-ELTE Protein Modeling Research Group at the Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, 1518, Budapest, Hungary.ORCID 0000-0002-9721-953X
Ernő KeszeiChemical Kinetics Laboratory, Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, 1518, Budapest, Hungary.
Pál StránerLaboratory of Structural Chemistry and Biology and, MTA-ELTE Protein Modeling Research Group at the Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, 1518, Budapest, Hungary.
Viktor FarkasLaboratory of Structural Chemistry and Biology and, MTA-ELTE Protein Modeling Research Group at the Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, 1518, Budapest, Hungary.
Gábor K TóthDepartment of Medical Chemistry, Faculty of General Medicine, University of Szeged, Szeged Dóm tér 8, H-6720, Szeged, Hungary.
András PerczelLaboratory of Structural Chemistry and Biology and, MTA-ELTE Protein Modeling Research Group at the Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, 1518, Budapest, Hungary.ORCID 0000-0002-9860-2215

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new approach to monitor disulfide-bond reduction in the vicinity of aromatic cluster(s) has been derived by using the near-UV range (λ=266-293 nm) of electronic circular dichroism (ECD) spectra. By combining the results from NMR and ECD spectroscopy, the 3D fold characteristics and associated reduction rate constants (k) of E19_SS, which is a highly thermostable, disulfide-bond reinforced 39-amino acid long exenatide mimetic, and its N-terminally truncated derivatives have been determined under different experimental conditions. Single disulfide bond reduction of the E19_SS model (with an 18-fold excess of tris(2-carboxyethyl)phosphine, pH 7, 37 °C) takes hours, which is 20-30 times longer than that expected, and thus, would not reach completion by applying commonly used reduction protocols. It is found that structural, steric, and electrostatic factors influence the reduction rate, resulting in orders of magnitude differences in reduction half-lives (900>t

Indexed as

Protein FoldingAmino Acid SequenceKineticsProtein DomainsProteinsTryptophanProteinsTryptophanaggregationkineticsprotein modelsreductionsulfur

Identifiers

PMID31475422
PMCPMC7079008

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