期刊
NANO LETTERS
卷 9, 期 12, 页码 4489-4493出版社
AMER CHEMICAL SOC
DOI: 10.1021/nl902803m
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资金
- National Natural Science Foundation of China [20735003, 20975098]
Na+-K+ ATPases have been observed and located by in situ AFM and single molecule recognition technique, topography and recognition imaging (TREC) that is a unique technique to specifically identify single protein in complex during AFM imaging. Na+-K+ ATPases were well distributed in the inner leaflet of cell membranes with about 10% aggregations in total recognized proteins. The height of Na+-K+ ATPases measured by AFM is in the range of 12-14 nm, which is very consistent with the cryoelectron microscopy result. The unbinding force between Na+-K+ ATPases in the membrane and anti-ATPases on the AFM tip is about 80 pN with the apparent loading rate at 40 nN/s. Our results show the first visualization of an essential membrane protein, Na+-K+ ATPase, in quasi-native cell membranes and may be significant to reveal the interactions between Na+-K+ ATPases and other membrane proteins at the molecular level.
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