Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorMukhopadhyay, Sabyasachien_US
dc.contributor.authorKaruppannan, Senthil Kumaren_US
dc.contributor.authorGuo, Cunlanen_US
dc.contributor.authorFereiro, Jerry A.en_US
dc.contributor.authorBergren, Adamen_US
dc.contributor.authorMukundan, Vineethaen_US
dc.contributor.authorQiu, Xinkaien_US
dc.contributor.authorCastañeda Ocampo, Olga E.en_US
dc.contributor.authorChen, Xiaopingen_US
dc.contributor.authorChiechi, Ryan C.en_US
dc.contributor.authorMcCreery, Richarden_US
dc.contributor.authorPecht, Israelen_US
dc.contributor.authorSheves, Mordechaien_US
dc.contributor.authorPasula, Rupali Reddyen_US
dc.contributor.authorLim, Sierinen_US
dc.contributor.authorNijhuis, Christian A.en_US
dc.contributor.authorVilan, Ayeleten_US
dc.contributor.authorCahen, Daviden_US
dc.identifier.citationMukhopadhyay, S., Karuppannan, S. K., Guo, C., Fereiro, J. A., Bergren, A., Mukundan, V., . . . Cahen, D. (2020). Solid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic coupling. iScience, 23(5), 101099-. doi:10.1016/j.isci.2020.101099en_US
dc.description.abstractSuccessful integration of proteins in solid-state electronics requires contacting them in a non-invasive fashion, with a solid conducting surface for immobilization as one such contact. The contacts can affect and even dominate the measured electronic transport. Often substrates, substrate treatments, protein immobilization, and device geometries differ between laboratories. Thus the question arises how far results from different laboratories and platforms are comparable and how to distinguish genuine protein electronic transport properties from platform-induced ones. We report a systematic comparison of electronic transport measurements between different laboratories, using all commonly used large-area schemes to contact a set of three proteins of largely different types. Altogether we study eight different combinations of molecular junction configurations, designed so that Ageoof junctions varies from 105 to 10-3 μm2. Although for the same protein, measured with similar device geometry, results compare reasonably well, there are significant differences in current densities (an intensive variable) between different device geometries. Likely, these originate in the critical contact-protein coupling (∼contact resistance), in addition to the actual number of proteins involved, because the effective junction contact area depends on the nanometric roughness of the electrodes and at times, even the proteins may increase this roughness. On the positive side, our results show that understanding what controls the coupling can make the coupling a design knob. In terms of extensive variables, such as temperature, our comparison unanimously shows the transport to be independent of temperature for all studied configurations and proteins. Our study places coupling and lack of temperature activation as key aspects to be considered in both modeling and practice of protein electronic transport experiments.en_US
dc.description.sponsorshipMinistry of Education (MOE)en_US
dc.rights© 2020 The Author(s). This is an open access article under the CC BY-NC-ND license (
dc.subjectEngineering::Chemical engineeringen_US
dc.titleSolid-state protein junctions : cross-laboratory study shows preservation of mechanism at varying electronic couplingen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.description.versionPublished versionen_US
dc.subject.keywordsElectronic Couplingen_US
dc.description.acknowledgementS.M. thanks SERB-DST, Govt. of India (award No. ECR/2017/001937 ) research grants, and the Council for Higher Education (Israel) for a postdoctoral research fellowship at the initial stage of this work. J.F. thanks the Azrieli Foundation for a PD fellowship; C.G. acknowledges a Dean's PD fellowship. At WIS, we thank Dr. Noga Friedman for bR samples, the Minerva Foundation (Munich) and the Israel Science Foundation for partial support. NUS research groups acknowledge the Ministry of Education (MOE) for supporting this research under award No. MOE2015-T2-2-134. Prime Minister’s Office, Singapore, under its medium-sized centre program, is also acknowledged for supporting this research. At Groningen the Zernike Institute of Advanced Materials is gratefully acknowledged for financial support. R.M. thanks the Zernike Institute of Advanced Materials; R.C. and V.M. thank the University of Alberta & Alberta Innovates, and R.C. and A.B. thank the National Research Council Canada for financial support.en_US
item.fulltextWith Fulltext-
Appears in Collections:SCBE Journal Articles
Files in This Item:
File Description SizeFormat 
PIIS2589004220302844.pdf5.86 MBAdobe PDFView/Open

Citations 50

Updated on Mar 10, 2021

Page view(s)

Updated on Apr 14, 2021


Updated on Apr 14, 2021

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.