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Jens Enevold Thaulov Andersen

Researcher at Botswana International University of Science and Technology

Publications -  116
Citations -  2300

Jens Enevold Thaulov Andersen is an academic researcher from Botswana International University of Science and Technology. The author has contributed to research in topics: Scanning tunneling microscope & Azurin. The author has an hindex of 23, co-authored 114 publications receiving 2171 citations. Previous affiliations of Jens Enevold Thaulov Andersen include University of Copenhagen & Technical University of Denmark.

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Molecular Monolayers and Interfacial Electron Transfer of Pseudomonas aeruginosa Azurin on Au(111)

TL;DR: In this paper, the formation and characterization of molecular monolayers of the blue copper protein Pseudomonas aeruginosa azurin on Au(111) in aqueous ammonium acetate solution was provided.
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Ordered Assembly and Controlled Electron Transfer of the Blue Copper Protein Azurin at Gold (111) Single-Crystal Substrates

TL;DR: In this paper, Pseudomonas aeruginosa azurin can be immobilized on alkanethiol monolayers self-assembled on Au(111) by hydrophobic interactions.
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Two-Dimensional Cysteine and Cystine Cluster Networks on Au(111) Disclosed by Voltammetry and in Situ Scanning Tunneling Microscopy

TL;DR: In this article, high-resolution STM images show that the adlayers of both cyteine and cystine exhibit highly-ordered networklike clusters with (3√3 × 6)R30° structure.
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Electronic properties of functional biomolecules at metal/aqueous solution interfaces

TL;DR: In this article, in situ scanning tunneling microscopy (STM) is used to explore single-molecule electronic properties directly in aqueous solution, which is a new dimension in interfacial bioelectrochemistry.
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An approach to long-range electron transfer mechanisms in metalloproteins: In situ scanning tunneling microscopy with submolecular resolution

TL;DR: Well resolved in situ STM images show arrays of molecules on the triangular gold(111) terraces that support the notion of tunneling via the redox level of the copper atom and of in situSTM as a new approach to long-range electron tunneling in metalloproteins.