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Atomic force microscopy imaging of the structure of the motor protein prestin reconstituted into an artificial lipid bilayer
Author(s) -
Kumano Shun,
Murakoshi Michio,
Iida Koji,
Hamana Hiroshi,
Wada Hiroshi
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.076
Subject(s) - prestin , motor protein , chemistry , cytoplasm , lipid bilayer , biophysics , bilayer , chinese hamster ovary cell , microbiology and biotechnology , biochemistry , membrane , biology , receptor , microtubule
Prestin is the motor protein of cochlear outer hair cells and is essential for mammalian hearing. The present study aimed to clarify the structure of prestin by atomic force microscopy (AFM). Prestin was purified from Chinese hamster ovary cells which had been modified to stably express prestin, and then reconstituted into an artificial lipid bilayer. Immunofluorescence staining with anti‐prestin antibody showed that the cytoplasmic side of prestin was possibly face up in the reconstituted lipid bilayer. AFM observation indicated that the cytoplasmic surface of prestin was ring‐like with a diameter of about 11 nm.