Single protein pores containing molecular adapters at high temperatures.
Bearing the heat: Current has been measured from individual protein pores at temperatures approaching 100°C. The molecular adapter β-cyclodextrin (red) remains bound to the α-hemolysin pore at high temperatures and retains the ability to bind guest molecules (black). Recording current at high temper...
Main Authors: | Kang, X, Gu, L, Cheley, S, Bayley, H |
---|---|
格式: | Journal article |
語言: | English |
出版: |
2005
|
相似書籍
-
Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.
由: Gu, L, et al.
出版: (2000) -
Single DNA rotaxanes of a transmembrane pore protein.
由: Sánchez-Quesada, J, et al.
出版: (2004) -
Redirecting pore assembly of staphylococcal α-hemolysin by protein engineering
由: Koo, S, et al.
出版: (2019) -
Partitioning of individual flexible polymers into a nanoscopic protein pore.
由: Movileanu, L, et al.
出版: (2003) -
A protein pore with a single polymer chain tethered within the lumen
由: Howorka, S, et al.
出版: (2000)