title: Site-specific incorporation of chemical probes into proteins for NMR.
abstract: The ability to incorporate chemical probes into peptides is of great importance because it can render novel functionality to proteins and greatly expand our capacity to investigate complex biological systems. A methodology developed by the Schultz laboratory provides a unique strategy to incorporate chemical probes as unnatural amino acids into proteins by "expanding the genetic code" of the host cell. A recent application of this methodology that allows the site-specific incorporation of three NMR-active probes into proteins demonstrates the potential for researchers to explore avenues that are not easily achievable with existing methods.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. aqhassan@mit.edu
authors.forename: A Quamrul
authors.initials: AQ
authors.lastname: Hassan
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry / Q000378:metabolism; D002247:Carbon Isotopes; D018389:Codon, Nonsense / Q000737:chemistry; D064429:Fatty Acid Synthases / Q000737:chemistry* / Q000235:genetics; D005461:Fluorine; D016297:Mutagenesis, Site-Directed; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry; D014443:Tyrosine / Q000031:analogs & derivatives / Q000737:chemistry
chemical_list: D000596:Amino Acids; D002247:Carbon Isotopes; D018389:Codon, Nonsense; D009587:Nitrogen Isotopes; D005461:Fluorine; D014443:Tyrosine; D010649:Phenylalanine; D064429:Fatty Acid Synthases; D000604:Amino Acyl-tRNA Synthetases