title: Protein semisynthesis and expressed protein ligation: chasing a protein's tail.
abstract: The adaptation of native chemical ligation to protein semisynthesis has become a powerful way to address problems in the analysis of protein structure and function. In particular, the exploitation of nature's inteins in expressed protein ligation is now a standard approach in the study of proteins. Site-specific incorporation of unnatural amino acids, biophysical probes and post-translational modifications in proteins have led to new insights into enzyme mechanisms, protein folding, ion channel function, translation and signaling.
authors.affiliation: Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Dirk
authors.initials: D
authors.lastname: Schwarzer
authors.forename: Philip A
authors.initials: PA
authors.lastname: Cole
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D047068:Arylalkylamine N-Acetyltransferase / Q000737:chemistry; D001430:Bacteriocins / Q000096:biosynthesis / Q000737:chemistry; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry; D010766:Phosphorylation; D015221:Potassium Channels / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D017368:Protein Prenylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012264:Ribonucleotide Reductases / Q000737:chemistry / Q000378:metabolism; D016335:Zinc Fingers / Q000235:genetics
chemical_list: D000596:Amino Acids; D001430:Bacteriocins; D010446:Peptide Fragments; D015221:Potassium Channels; D011506:Proteins; D011994:Recombinant Proteins; D012264:Ribonucleotide Reductases; D047068:Arylalkylamine N-Acetyltransferase; D012259:Ribonuclease, Pancreatic