Philip E. Dawson

TL;DR: The technique of native chemical ligation is employable for chemically synthesizing full length proteins as discussed by the authors, which are chemically identical to proteins produced by cell free synthesis, and can be refolded and/or oxidized to form native disulfide-containing protein molecules.

TL;DR: The facile access to novel analogs provided by chemical protein synthesis has led to original insights into the molecular basis of protein function in a number of systems.

TL;DR: A straightforward methodology that has enabled us to rapidly analyze the compatibility of the native chemical ligation strategy for X-Cys ligation sites, where X is any of the 20 naturally occurring amino acids, and shows that all 20 amino acids are suitable for ligation.

TL;DR: This approach, which provides a general method to prepare alanyl proteins from their cysteinyl forms, can be used to chemically synthesize a variety of polypeptides, as demonstrated by the total chemical syntheses of the cyclic antibiotic microcin J25, the 56-amino acid streptococcal protein G B1 domain, and a variant of the 110-amINO acid ribonuclease, barnase.

TL;DR: Luminescent quantum dot bioconjugates designed to detect proteolytic activity by fluorescence resonance energy transfer are presented, not limited to sensing proteases, but may be amenable to monitoring other enzymatic modifications.