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A powerful technology called global protein stability profiling allows rates of protein turnover to be determined for a substantial fraction of the human proteome in a single experiment. This approach sets the stage for systems-level analyses of the dynamics of the mammalian proteome.
Cytochrome P450 enzymes selectively oxidize relatively unactivated sites in a range of model drug-like substrates in vitro. The hydroxylated products can be transformed into selectively fluorinated systems, providing a rapid sequential method for the identification, activation and fluorination of saturated sites in drug candidates.
Protein ubiquitination is an important degradative signal, yet not all ubiquitinated proteins are degraded. Recent results reveal insights into the proteasome's strategy for integrating biophysical signals when choosing substrates for degradation.
Peptidases are enzymes that trim small protein fragments called peptides to regulate their biological functions. A new method opens the door to chasing down and identifying important cutting events mediated by peptidases involved in metabolic regulation.
