Zachary A Knight1, Birgit Schilling2, Richard H Row2, Denise M Kenski1, Bradford W Gibson2, 3
& Kevan M Shokat4, 51
Program in Chemistry and Chemical Biology,
University of California, San Francisco, California,
USA.
2
The Buck Institute for Age Research,
8001 Redwood Boulevard, Novato, California
94945, USA.
3
Department of Pharmaceutical Chemistry, University
of California, Box 0446, San Francisco, California
94143-0446, USA.
4
Department of Cellular and Molecular Pharmacology,
Box 2280, University of California, San Francisco,
California 94143-2280, USA.
5
Department of Chemistry, University of
California, Berkeley, California
94720-1460, USA.
Correspondence should be addressed to Kevan M Shokat shokat@cmp.ucsf.edu
-methylaminoethylcysteine, respectively).
Aminoethylcysteine-modified peptides are then cleaved with a lysine-specific
protease to map sites of phosphorylation. A blocking step enables single-site
cleavage, and adaptation of this reaction to the solid phase facilitates
phosphopeptide enrichment and modification in one step.
s is palmitoylated at the N-terminal glycine
