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Atomic‐Force‐Microscopy Imaging and Molecular‐Recognition‐Force Microscopy of Recrystallized Heterotetramers Comprising an S‐Layer‐Streptavidin Fusion Protein
Author(s) -
Ebner Andreas,
Kienberger Ferry,
Huber Carina,
Kamruzzahan A. S. M.,
Pastushenko Vassili Ph.,
Tang Jilin,
Kada Gerald,
Gruber Hermann J.,
Sleytr Uwe B.,
Sára Margit,
Hinterdorfer Peter
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500445
Subject(s) - force spectroscopy , streptavidin , microscopy , atomic force microscopy , biophysics , scanning force microscopy , molecule , chemistry , s layer , fusion , crystallography , fusion protein , materials science , nanotechnology , biology , biochemistry , physics , biotin , optics , recombinant dna , linguistics , philosophy , gene , organic chemistry
Add‐on features . S‐layer proteins reassemble on surfaces to form 2D crystals with lattice constants in the nanometer range. By modifying these proteins with capture molecules through genetic engineering, specific binding sites, such as streptavidin tags, can be introduced. The activity of these sites is proven by single‐molecule recognition‐force spectroscopy. In addition, structural details of the morphological units were resolved by using dynamic force microscopy imaging.