Please use this identifier to cite or link to this item: doi:10.22028/D291-28894
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Title: Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein
Author(s): Griffo, Alessandra
Hähl, Hendrik
Grandthyll, Samuel
Müller, Frank
Paananen, Arja
Ilmén, Marja
Szilvay, Géza R.
Landowski, Christopher P.
Penttilä, Merja
Jacobs, Karin
Laaksonen, Päivi
Language: English
Title: ACS Omega
Volume: 2
Issue: 10
Startpage: 6906
Endpage: 6915
Publisher/Platform: American Chemical Society (ACS)
Year of Publication: 2017
Publikation type: Journal Article
Abstract: The adhesive and mechanical properties of a modular fusion protein consisting of two different types of binding units linked together via a flexible resilin-like-polypeptide domain are quantified. The adhesive domains have been constructed from fungal cellulose-binding modules (CBMs) and an amphiphilic hydrophobin HFBI. This study is carried out by single-molecule force spectroscopy, which enables stretching of single molecules. The fusion proteins are designed to self-assemble on the cellulose surface, leading into the submonolayer of proteins having the HFBI pointing away from the surface. A hydrophobic atomic force microscopy (AFM) tip can be employed for contacting and lifting the single fusion protein from the HFBI-functionalized terminus by the hydrophobic interaction between the tip surface and the hydrophobic patch of the HFBI. The work of rupture, contour length at rupture and the adhesion forces of the amphiphilic end domains are evaluated under aqueous environment at different pHs.
DOI of the first publication: 10.1021/acsomega.7b01133
Link to this record: hdl:20.500.11880/27773
http://dx.doi.org/10.22028/D291-28894
ISSN: 2470-1343
2470-1343
Date of registration: 13-Sep-2019
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Department: NT - Physik
Collections:UniBib – Die Universitätsbibliographie

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