Evidence map›Paper›PMID 33024651›Full record

ArticleChemistryOpen2020

L-Lysine Amino Acid Adsorption on Zeolite L: a Combined Synchrotron, X-Ray and Neutron Diffraction Study.

Giada Beltrami, Annalisa Martucci, Luisa Pasti, Tatiana Chenet, Matteo Ardit, Lara Gigli, Mirco Cescon, Emmanuelle Suard

Open access · goldAbstract read
In one paragraph

Article in ChemistryOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 13 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Giada BeltramiDepartment of Physics and Earth Sciences, University of Ferrara, Via Saragat 1, 44121, Ferrara, Italy.
Annalisa MartucciDepartment of Physics and Earth Sciences, University of Ferrara, Via Saragat 1, 44121, Ferrara, Italy.ORCID http://orcid.org/0000-0002-6467-881X
Luisa PastiDipartimento di Scienze Chimiche e Farmaceutiche, University of Ferrara, Via Fossato di Mortara 17, 44121, Ferrara, Italy.
Tatiana ChenetDipartimento di Scienze Chimiche e Farmaceutiche, University of Ferrara, Via Fossato di Mortara 17, 44121, Ferrara, Italy.
Matteo ArditDepartment of Physics and Earth Sciences, University of Ferrara, Via Saragat 1, 44121, Ferrara, Italy.
Lara GigliElettra-Sincrotrone Trieste S.C.p.A., Materials Characterisation by X-ray diffraction (MCX) beamline Strada, Statale, 14 - km 163,5 in AREA Science Park, Basovizza, Trieste, Italy.
Mirco CesconDipartimento di Scienze Chimiche e Farmaceutiche, University of Ferrara, Via Fossato di Mortara 17, 44121, Ferrara, Italy.
Emmanuelle SuardInstitute Max Von Laue and Paul Langevin, D2B beamline BP156, 38042, Grenoble, France.
University of Ferrara · ITElettra-Sincrotrone Trieste S.C.p.A. · ITInstitut Langevin · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Combined neutron and X-ray powder diffraction techniques highlighted the sorption capacity of the acidic L zeolite towards the L-lysine amino acid. The role of zeolite channels in the stabilization of the lysine absorbed and the effect of water on protein structure are elucidated at atomistic level. The stabilization of the L α-helical conformation is related to strong H-bonds between the tail aminogroups of lysine molecules and the Brønsted acid site as well as to complex intermolecular H-bond system between water molecules, zeolite and amino acid. This finding is relevant in the catalytic synthesis of polypeptide, as well as in industrial biotechnology by qualitatively predicting binding behaviour.

Indexed as

Neutron DiffractionSynchrotronsX-Ray DiffractionAdsorptionHydrogen BondingLysineProtein StabilityZeolitesLysineZeolitesBrønsted acid siteL-lysine adsorptionL zeoliteneutron and synchrotron X-ray diffractionα-helical conformation

Identifiers

PMID33024651
PMCPMC7528762
OpenAlexW3088336325

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.