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Exploring the Conformation‐Regulated Function of Titin Kinase by Mechanical Pump and Probe Experiments with Single Molecules
Author(s) -
Puchner Elias M.,
Gaub Hermann E.
Publication year - 2010
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.200905956
Subject(s) - titin , function (biology) , atomic force microscopy , nanotechnology , molecule , chemistry , biophysics , enzyme , computational biology , materials science , biochemistry , microbiology and biotechnology , biology , myocyte , sarcomere , organic chemistry
Feel the force : A new AFM‐based single‐molecule pump‐and‐probe protocol has been used to investigate the function of different force‐induced conformations of proteins (see picture). It was found that the autoinhibited enzyme titin kinase reaches its ability to bind ATP after the first two barriers of the complex mechanical activation pathway.

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