Site-specific incorporation of chemical probes into proteins for NMR.
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.
Hassan
A Quamrul
AQ
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. aqhassan@mit.edu
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
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