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Light‐Triggered Myosin Activation for Probing Dynamic Cellular Processes
Author(s) -
Goguen Brenda N.,
Hoffman Brenton D.,
Sellers James R.,
Schwartz Martin A.,
Imperiali Barbara
Publication year - 2011
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.201100674
Subject(s) - myosin , phosphoserine , chemistry , biophysics , biochemistry , computational biology , nanotechnology , biology , phosphorylation , materials science , serine
Shining light on myosin : The incorporation of a caging group onto the essential phosphoserine residue of myosin by protein semisynthesis enables light‐triggered activation of the protein (see picture). Caging eliminates the myosin activity, but exposure to 365 nm light restores its function to native levels. The caged protein can also be introduced into cells to facilitate studies of myosin with precise spatial and temporal resolution.