Exploring the Conformation-Regulated Function of Titin Kinase by Mechanical Pump and Probe Experiments with Single Molecules

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 o...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2010-02, Vol.49 (6), p.1147-1150
Main Authors: Puchner, Elias M, Gaub, Hermann E
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
Connectin
enzymes
force spectroscopy
Humans
Microscopy, Atomic Force - methods
Models, Molecular
Muscle Proteins - analysis
Muscle Proteins - chemistry
Muscle Proteins - metabolism
Muscle Proteins - ultrastructure
Protein Binding
Protein Folding
Protein Kinases - analysis
Protein Kinases - chemistry
Protein Kinases - metabolism
Protein Kinases - ultrastructure
Protein Structure, Quaternary
Protein Structure, Tertiary
scanning probe microscopy
sensors
single-molecule studies
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200905956