N-Terminal Modification of Proteins witho-Aminophenols

N-Terminal Modification of Proteins with o-Aminophenols

The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on...

N-terminal protein modification through a biomimetic transamination reaction.

withO - the - Shelf RISC

Multithreaded architectures have been proposed for future multiprocessor systems due to their ability to cope with network and synchronization latencies. Some of these architectures depart signiicantly from current RISC processor designs, while others retain most of the RISC core unchanged. However, in light of the very low cost and excellent performance of oo-the-shelf microprocessors it seems...

Prediction of N-myristoylation modification of proteins by SVM

Attachment of a myristoyl group to NH(2)-terminus of a nascent protein among protein post-translational modification (PTM) is called myristoylation. The myristate moiety of proteins plays an important role for their biological functions, such as regulation of membrane binding (HIV-1 Gag) and enzyme activity (AMPK). Several predictors based on protein sequences alone are hitherto proposed. Howev...

N-terminal processing of proteins exported by malaria parasites.

Malaria parasites utilize a short N-terminal amino acid motif termed the Plasmodium export element (PEXEL) to export an array of proteins to the host erythrocyte during blood stage infection. Using immunoaffinity chromatography and mass spectrometry, insight into this signal-mediated trafficking mechanism was gained by discovering that the PEXEL motif is cleaved and N-acetylated. PfHRPII and Pf...