Evidence map›Paper›PMID 31546917›Full record

ArticleBiomolecules2019

Mechanical Deformation and Electronic Structure of a Blue Copper Azurin in a Solid-State Junction.

Carlos Romero-Muñiz, María Ortega, J G Vilhena, Ismael Diéz-Pérez, Juan Carlos Cuevas, Rubén Pérez, Linda A Zotti

Abstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

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

6 citing papers in PubMed.

  1. Electron transport through two interacting channels in Azurin-based solid-state junctions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Efficient Electron Hopping Transport through Azurin-Based Junctions.The journal of physical chemistry letters · 2023
    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.

Carlos Romero-MuñizDepartamento de Física Teórica de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain. carlos.romero@uam.es.ORCID 0000-0001-6902-1553
María OrtegaDepartamento de Física Teórica de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain. maria.ortega@uam.es.ORCID 0000-0002-3300-0053
J G VilhenaDepartment of Physics, University of Basel, Klingelbergstrasse 82, CH-4056 Basel, Switzerland. guilhermevilhena@gmail.com.ORCID 0000-0001-8338-9119
Ismael Diéz-PérezDepartment of Chemistry, Faculty of Natural & Mathematical Sciences, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, UK. ismael.diez_perez@kcl.ac.uk.ORCID 0000-0003-0513-8888
Juan Carlos CuevasDepartamento de Física Teórica de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain. juancarlos.cuevas@uam.es.ORCID 0000-0001-7421-0682
Rubén PérezDepartamento de Física Teórica de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain. ruben.perez@uam.es.ORCID 0000-0001-5896-541X
Linda A ZottiDepartamento de Física Teórica de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain. linda.zotti@uam.es.ORCID 0000-0002-5292-6759

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-based electronics is an emerging field which has attracted considerable attention over the past decade. Here, we present a theoretical study of the formation and electronic structure of a metal-protein-metal junction based on the blue-copper azurin from pseudomonas aeruginosa. We focus on the case in which the protein is adsorbed on a gold surface and is contacted, at the opposite side, to an STM (Scanning Tunneling Microscopy) tip by spontaneous attachment. This has been simulated through a combination of molecular dynamics and density functional theory. We find that the attachment to the tip induces structural changes in the protein which, however, do not affect the overall electronic properties of the protein. Indeed, only changes in certain residues are observed, whereas the electronic structure of the Cu-centered complex remains unaltered, as does the total density of states of the whole protein.

Indexed as

AdsorptionAzurinBiomechanical PhenomenaCopperDensity Functional TheoryElectron TransportGoldMicroscopy, Scanning TunnelingModels, MolecularMolecular Dynamics SimulationProtein Structure, TertiaryPseudomonas aeruginosaSurface PropertiesAzurinCopperGoldazurinbiomolecular electronicsdensity functional theoryelectronic transportmolecular dynamicssolid-state junction

Identifiers

PMID31546917
PMCPMC6769874

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Registered trials

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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.