25025-59-6Relevant articles and documents
Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications
Chalker, Justin M.,Lercher, Lukas,Rose, Nathan R.,Schofield, Christopher J.,Davis, Benjamin G.
supporting information; experimental part, p. 1835 - 1839 (2012/04/04)
Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.
Nucleophilic Esterolytic and Displacement Reactions of a Micellar Thiocholine Surfactant
Moss, Robert A.,Bizzigotti, George O.,Huang, Ching-Wen
, p. 754 - 762 (2007/10/02)
The thiol-functionalized surfactant N-n-cetyl-N,N-dimethyl-N-(β-thioethyl)ammonium chloride, 4 (16-SH), was synthesized.Under micellar conditions at pH 7, excess micellar 16-SH cleaved p-nitrophenyl acetate (PNPA) with kψmax = 2.16 s