Incorporation of selenocysteine into proteins using peptide ligation.
Expressed protein ligation has become a frequently used technique to insert non-standard amino acids into proteins. The technique has been adapted to insert selenocysteine residues in place of cysteine residue in proteins, taking advantage of the similarity in the chemistries of sulfur and selenium. This replacement can confer unique structural and catalytic properties to enzymes and proteins. The development of this technique also allows for naturally occurring selenoproteins to be produced semisynthetically.
Hondal
Robert J
RJ
Department of Biochemistry, Vermont College of Medicine, The University of Vermont, Burlington, VT 05405, USA. Robert.Hondal@uvm.edu
D000818:Animals; D001671:Biochemistry / Q000379:methods*; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D047668:Inteins; D008956:Models, Chemical; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics; D017279:Selenocysteine / Q000138:chemical synthesis / Q000737:chemistry*; D013880:Thioredoxin-Disulfide Reductase / Q000138:chemical synthesis / Q000737:chemistry
D010455:Peptides; D011506:Proteins; D017279:Selenocysteine; D013880:Thioredoxin-Disulfide Reductase; D012260:Ribonucleases