Posttranslational modification (PTM) is a key mechanism for regulating diverse protein functions, and thus critically affects many essential biological processes. Critical for systematic study of the effects of PTMs is the ability to obtain recombinant proteins with defined and homogenous modifications. To this end, various synthetic and chemical biology approaches, including genetic code expansion and protein chemical modification methods, have been developed. These methods have proven effective for generating site-specific authentic modifications or structural mimics, and have demonstrated their value for in vitro and in vivo functional studies of diverse PTMs. This review will discuss recent advances in chemical biology strategies and their application to various PTM studies.

We present a new platform for multiplexed protein kinase activity assay using TiO decorated graphene oxide (GO), which is applicable to high throughput inhibitor screening. On the basis of the strong affinity of TiO for the phosphate group and the fluorescence quenching capability of GO, phosphorylation of substrates by protein kinases was quantitatively measured in a short time.

No abstract