title: Semisynthetic proteins in mechanistic studies: using chemistry to go where nature can't.
abstract: The manipulation of the chemical structure of proteins beyond what is feasible with standard genetics, offers a powerful strategy to investigate protein mechanisms. By allowing the incorporation of biophysical probes, unnatural amino acids, and post-translational modifications in proteins, chemistry-driven approaches have greatly contributed to the understanding of the molecular basis of protein function.
authors.affiliation: The Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, NY 10021, USA.
authors.forename: Jean-Philippe
authors.initials: JP
authors.lastname: Pellois
authors.forename: Tom W
authors.initials: TW
authors.lastname: Muir
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D020558:GTP Phosphohydrolases / Q000737:chemistry; D006657:Histones / Q000737:chemistry; D007473:Ion Channels; D015335:Molecular Probes; D015202:Protein Engineering / Q000379:methods; D011499:Protein Processing, Post-Translational; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry* / Q000502:physiology; D012264:Ribonucleotide Reductases / Q000737:chemistry; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D006657:Histones; D007473:Ion Channels; D015335:Molecular Probes; D011506:Proteins; D012264:Ribonucleotide Reductases; D017027:Protein Tyrosine Phosphatases; D020558:GTP Phosphohydrolases