Evidence map›Paper›PMID 32309689›Full record

ArticleACS omega2020

Printed-Circuit-Board-Based Two-Electrode System for Electronic Characterization of Proteins.

Sara Talebi, Souhad M A Daraghma, Ramesh T Subramaniam, Subha Bhassu, Georgepeter Gnana Kumar, Vengadesh Periasamy

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
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

6 authors at 2 institutions in 2 countries.

Sara TalebiLow Dimensional Materials Research Centre (LDMRC), Department of Physics, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.
Souhad M A DaraghmaLow Dimensional Materials Research Centre (LDMRC), Department of Physics, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.
Ramesh T SubramaniamCentre for Ionics University of Malaya, Department of Physics, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.
Subha BhassuInstitute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.
Georgepeter Gnana KumarDepartment of Physical Chemistry, School of Chemistry, Madurai Kamaraj University, Madurai 625021, Tamil Nadu, India.
Vengadesh PeriasamyLow Dimensional Materials Research Centre (LDMRC), Department of Physics, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.
University of Malaya · MYMadurai Kamaraj University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins have been increasingly suggested as suitable candidates for the fabrication of biological computers and other biomolecular-based electronic devices mainly due to their interesting structure-related intrinsic electrical properties. These natural biopolymers are environmentally friendly substitutes for conventional inorganic materials and find numerous applications in bioelectronics. Effective manipulation of protein biomolecules allows for accurate fabrication of nanoscaled device dimensions for miniaturized electronics. The prerequisite, however, demands an interrogation of its various electronic properties prior to understanding the complex charge transfer mechanisms in protein molecules, the knowledge of which will be crucial toward development of such nanodevices. One significantly preferred method in recent times involves the utilization of solid-state sensors where interactions of proteins could be investigated upon contact with metals such as gold. Therefore, in this work, proteins (hemoglobin and collagen) were integrated within a two-electrode system, and the resulting electronic profiles were investigated. Interestingly, structure-related electronic profiles representing semiconductive-like behaviors were observed. These characteristic electronic profiles arise from the metal (Au)-semiconductor (protein) junction, clearly demonstrating the formation of a Schottky junction. Further interpretation of the electronic behavior of proteins was done by the calculation of selected solid-state parameters. For example, the turn-on voltage of hemoglobin was measured to occur at a lower turn-on voltage, indicating the possible influence of the hem group present as a cofactor in each subunit of this tetrameric protein.

Identifiers

PMID32309689
PMCPMC7160841
OpenAlexW3015052891

What OpenQuestion holds

Textmetadata
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.