title: Isotope labeling in insect cells.
abstract: Recent years have seen remarkable progress in applying nuclear magnetic resonance (NMR) spectroscopy to proteins that have traditionally been difficult to study due to issues with folding, posttranslational modification, and expression levels or combinations thereof. In particular, insect cells have proved useful in allowing large quantities of isotope-labeled, functional proteins to be obtained and purified to homogeneity, allowing study of their structures and dynamics by using NMR. Here, we provide protocols that have proven successful in such endeavors.
authors.affiliation: Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University Frankfurt, Frankfurt am Main, Germany.
authors.forename: Krishna
authors.initials: K
authors.lastname: Saxena
authors.forename: Arpana
authors.initials: A
authors.lastname: Dutta
authors.forename: Judith
authors.initials: J
authors.lastname: Klein-Seetharaman
authors.forename: Harald
authors.initials: H
authors.lastname: Schwalbe
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D016367:Baculoviridae; D019149:Bioreactors; D002460:Cell Line; D005822:Genetic Vectors / Q000235:genetics; D018832:Molecular Chaperones / Q000378:metabolism; D009587:Nitrogen Isotopes / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D018411:Spodoptera; D013696:Temperature; D014162:Transfection / Q000379:methods
chemical_list: D000596:Amino Acids; D018832:Molecular Chaperones; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins