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Single Protein Pores Containing Molecular Adapters at High Temperatures
Author(s) -
Kang Xiaofeng,
Gu LiQun,
Cheley Stephen,
Bayley Hagan
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200461885
Subject(s) - adapter (computing) , molecule , chemistry , biophysics , materials science , nanotechnology , chemical physics , organic chemistry , computer science , biology , operating system
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 temperatures is likely to be important for the study of single‐molecule chemistry and in the development of stochastic sensors.