Selenoprotein Structure and Function, Volume 662 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters written by an international board of authors. Chapters in this new release include Identification of Selenoprotein O substrates using a biotinylated ATP analog, Selenium-encoded isotopic signature targeted profiling, Designing tRNASec variants for efficient selenocysteine incorporation using Sec-specific reporters, Preparation of selenoprotein S by chemical ligation, Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells, SecMS analysis of selenoprotein with selenocysteine insertion sequence and beyond, Selenocysteine substitutions in thiyl radical enzymes, and much more.
Additional chapters cover Recombinant selenoprotein expression in E. coli based upon the redefinition of a UAG codon in an RF1-depleted host strain, Metabolic labeling with radioactive selenium in zebrafish, Low pH isoTOP-ABPP to identify selenocysteines, Expression of selenoproteins via genetic code expansion in mammalian cells, Alpha-methyl selenocysteine as a tool for the study of selenoproteins, Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications, and much more.
1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Series Page - p. iii 5. Copyright - p. iii 6. Contributors - p. iii 7. Preface - p. xv 8. Chapter One: Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells - p. 1 9. Chapter Two: Methods for accurate and reproducible studies of pharmacological effects of selenium in cancer - p. 25 10. Chapter Three: Using selenocysteine-specific reporters to screen for efficient tRNASec variants - p. 63 11. Chapter Four: Expressing recombinant selenoproteins using redefinition of a single UAG codon in an RF1-depleted E. coli host strain - p. 95 12. Chapter Five: Selenocysteine substitutions in thiyl radical enzymes - p. 119 13. Chapter Six: Expression of selenoproteins via genetic code expansion in mammalian cells - p. 143 14. Chapter Seven: Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S - p. 159 15. Chapter Eight: Chemoproteomic interrogation of selenocysteine by low-pH isoTOP-ABPP - p. 207 16. Chapter Nine: SecMS analysis of selenoproteins with selenocysteine insertion sequence and beyond - p. 227 17. Chapter Ten: An accelerated and optimized algorithm of selenium-encoded isotopic signature targeted profiling for global selenoproteome analysis - p. 241 18. Chapter Eleven: Assay of selenol species in biological samples by the fluorescent probe Sel-green - p. 259 19. Chapter Twelve: Identification of selenoprotein O substrates using a biotinylated ATP analog - p. 275 20. Chapter Thirteen: Application of alpha-methyl selenocysteine as a tool for the study of selenoproteins - p. 297 21. Chapter Fourteen: Modeling of selenocysteine-derived reactive intermediates utilizing a nano-sized molecular cavity as a protective cradle - p. 331 22. Chapter Fifteen: Diselenide-selenoester ligation in the chemical synthesis of proteins - p. 363
Selenoprotein Structure and Function, Volume 662 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters written by an international board of authors. Chapters in this new release include Identification of Selenoprotein O substrates using a biotinylated ATP analog, Selenium-encoded isotopic signature targeted profiling, Designing tRNASec variants for efficient selenocysteine incorporation using Sec-specific reporters, Preparation of selenoprotein S by chemical ligation, Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells, SecMS analysis of selenoprotein with selenocysteine insertion sequence and beyond, Selenocysteine substitutions in thiyl radical enzymes, and much more.
Additional chapters cover Recombinant selenoprotein expression in E. coli based upon the redefinition of a UAG codon in an RF1-depleted host strain, Metabolic labeling with radioactive selenium in zebrafish, Low pH isoTOP-ABPP to identify selenocysteines, Expression of selenoproteins via genetic code expansion in mammalian cells, Alpha-methyl selenocysteine as a tool for the study of selenoproteins, Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications, and much more.
1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Series Page - p. iii 5. Copyright - p. iii 6. Contributors - p. iii 7. Preface - p. xv 8. Chapter One: Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells - p. 1 9. Chapter Two: Methods for accurate and reproducible studies of pharmacological effects of selenium in cancer - p. 25 10. Chapter Three: Using selenocysteine-specific reporters to screen for efficient tRNASec variants - p. 63 11. Chapter Four: Expressing recombinant selenoproteins using redefinition of a single UAG codon in an RF1-depleted E. coli host strain - p. 95 12. Chapter Five: Selenocysteine substitutions in thiyl radical enzymes - p. 119 13. Chapter Six: Expression of selenoproteins via genetic code expansion in mammalian cells - p. 143 14. Chapter Seven: Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S - p. 159 15. Chapter Eight: Chemoproteomic interrogation of selenocysteine by low-pH isoTOP-ABPP - p. 207 16. Chapter Nine: SecMS analysis of selenoproteins with selenocysteine insertion sequence and beyond - p. 227 17. Chapter Ten: An accelerated and optimized algorithm of selenium-encoded isotopic signature targeted profiling for global selenoproteome analysis - p. 241 18. Chapter Eleven: Assay of selenol species in biological samples by the fluorescent probe Sel-green - p. 259 19. Chapter Twelve: Identification of selenoprotein O substrates using a biotinylated ATP analog - p. 275 20. Chapter Thirteen: Application of alpha-methyl selenocysteine as a tool for the study of selenoproteins - p. 297 21. Chapter Fourteen: Modeling of selenocysteine-derived reactive intermediates utilizing a nano-sized molecular cavity as a protective cradle - p. 331 22. Chapter Fifteen: Diselenide-selenoester ligation in the chemical synthesis of proteins - p. 363
