Electrical transport through ordered self-assembled protein monolayer measured by constant force conductive atomic force microscopy

Jani Kivioja (Corresponding Author), Katri Kurppa, Markku Kainlauri, Markus Linder, Jouni Ahopelto

    Research output: Contribution to journalArticleScientificpeer-review

    11 Citations (Scopus)

    Abstract

    This paper addresses some of the challenges met in electrical characterization of biomolecules, namely, the control of the orientation of molecules and the control of the force exerted on these soft molecules. We investigate the transport properties of small proteins called hydrophobins using conductive atomic force microscopy. The proteins have a property that they form a well ordered monolayer in which the orientation of the molecules is known. We introduce an active compensation for the electrostatic force induced by the bias voltage, which often hamper the measurements. Results suggest that the electrical transport through the hydrophobins protein monolayer occurs mainly via tunneling.
    Original languageEnglish
    Article number183901
    JournalApplied Physics Letters
    Volume94
    Issue number18
    DOIs
    Publication statusPublished - 2009
    MoE publication typeA1 Journal article-refereed

    Fingerprint

    atomic force microscopy
    proteins
    molecules
    transport properties
    electrostatics
    electric potential

    Keywords

    • electrical characterization
    • biomolecules
    • hydrophobin monolayer
    • hydrophobins

    Cite this

    @article{c94bd75593644c6bb5303d850b4098b5,
    title = "Electrical transport through ordered self-assembled protein monolayer measured by constant force conductive atomic force microscopy",
    abstract = "This paper addresses some of the challenges met in electrical characterization of biomolecules, namely, the control of the orientation of molecules and the control of the force exerted on these soft molecules. We investigate the transport properties of small proteins called hydrophobins using conductive atomic force microscopy. The proteins have a property that they form a well ordered monolayer in which the orientation of the molecules is known. We introduce an active compensation for the electrostatic force induced by the bias voltage, which often hamper the measurements. Results suggest that the electrical transport through the hydrophobins protein monolayer occurs mainly via tunneling.",
    keywords = "electrical characterization, biomolecules, hydrophobin monolayer, hydrophobins",
    author = "Jani Kivioja and Katri Kurppa and Markku Kainlauri and Markus Linder and Jouni Ahopelto",
    year = "2009",
    doi = "10.1063/1.3126448",
    language = "English",
    volume = "94",
    journal = "Applied Physics Letters",
    issn = "0003-6951",
    number = "18",

    }

    Electrical transport through ordered self-assembled protein monolayer measured by constant force conductive atomic force microscopy. / Kivioja, Jani (Corresponding Author); Kurppa, Katri; Kainlauri, Markku; Linder, Markus; Ahopelto, Jouni.

    In: Applied Physics Letters, Vol. 94, No. 18, 183901, 2009.

    Research output: Contribution to journalArticleScientificpeer-review

    TY - JOUR

    T1 - Electrical transport through ordered self-assembled protein monolayer measured by constant force conductive atomic force microscopy

    AU - Kivioja, Jani

    AU - Kurppa, Katri

    AU - Kainlauri, Markku

    AU - Linder, Markus

    AU - Ahopelto, Jouni

    PY - 2009

    Y1 - 2009

    N2 - This paper addresses some of the challenges met in electrical characterization of biomolecules, namely, the control of the orientation of molecules and the control of the force exerted on these soft molecules. We investigate the transport properties of small proteins called hydrophobins using conductive atomic force microscopy. The proteins have a property that they form a well ordered monolayer in which the orientation of the molecules is known. We introduce an active compensation for the electrostatic force induced by the bias voltage, which often hamper the measurements. Results suggest that the electrical transport through the hydrophobins protein monolayer occurs mainly via tunneling.

    AB - This paper addresses some of the challenges met in electrical characterization of biomolecules, namely, the control of the orientation of molecules and the control of the force exerted on these soft molecules. We investigate the transport properties of small proteins called hydrophobins using conductive atomic force microscopy. The proteins have a property that they form a well ordered monolayer in which the orientation of the molecules is known. We introduce an active compensation for the electrostatic force induced by the bias voltage, which often hamper the measurements. Results suggest that the electrical transport through the hydrophobins protein monolayer occurs mainly via tunneling.

    KW - electrical characterization

    KW - biomolecules

    KW - hydrophobin monolayer

    KW - hydrophobins

    U2 - 10.1063/1.3126448

    DO - 10.1063/1.3126448

    M3 - Article

    VL - 94

    JO - Applied Physics Letters

    JF - Applied Physics Letters

    SN - 0003-6951

    IS - 18

    M1 - 183901

    ER -