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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.
This volume provides a collection of contemporary perspectives on
using activity-based protein profiling (ABPP) for biological
discoveries in protein science, microbiology, and immunology. A
common theme throughout is the special utility of ABPP to
interrogate protein function and small-molecule interactions on a
global scale in native biological systems. Each chapter showcases
distinct advantages of ABPP applied to diverse protein classes and
biological systems. As such, the book offers readers valuable
insights into the basic principles of ABPP technology and how to
apply this approach to biological questions ranging from the study
of post-translational modifications to targeting bacterial
effectors in host-pathogen interactions.
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