title: Techniques for the analysis of cysteine sulfhydryls and oxidative protein folding.
abstract: CONCLUSIONS
  Modification of cysteine thiols dramatically affects protein function and stability. Hence, the abilities to quantify specific protein sulfhydryl groups within complex biological samples and map disulfide bond structures are crucial to gaining greater insights into how proteins operate in human health and disease.
  
  
  BACKGROUND
  Many different molecular probes are now commercially available to label and track cysteine residues at great sensitivity. Coupled with mass spectrometry, stable isotope-labeled sulfhydryl-specific reagents can provide previously unprecedented molecular insights into the dynamics of cysteine modification. Likewise, the combined application of modern mass spectrometers with improved sample preparation techniques and novel data mining algorithms is beginning to routinize the analysis of complex protein disulfide structures.
  
  
  RESULTS
  Proper application of these modern tools and techniques, however, still requires fundamental understanding of sulfhydryl chemistry as well as the assumptions that accompany sample preparation and underlie effective data interpretation.
  
  
  CONCLUSIONS
  The continued development of tools, technical approaches, and corresponding data processing algorithms will, undoubtedly, facilitate site-specific protein sulfhydryl quantification and disulfide structure analysis from within complex biological mixtures with ever-improving accuracy and sensitivity. Fully routinizing disulfide structure analysis will require an equal but balanced focus on sample preparation and corresponding mass spectral dataset reproducibility.
authors.affiliation: Center for Personalized Diagnostics, The Biodesign Institute at Arizona State University , Tempe, Arizona.
authors.forename: Chad R
authors.initials: CR
authors.lastname: Borges
authors.forename: Nisha D
authors.initials: ND
authors.lastname: Sherma
mesh_terms: D003545:Cysteine / Q000032:analysis / Q000737:chemistry*; D004220:Disulfides / Q000032:analysis / Q000737:chemistry*; D006801:Humans; D013058:Mass Spectrometry; D015335:Molecular Probes / Q000737:chemistry; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013438:Sulfhydryl Compounds / Q000032:analysis / Q000737:chemistry; D013439:Sulfhydryl Reagents / Q000737:chemistry
chemical_list: D004220:Disulfides; D015335:Molecular Probes; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; D003545:Cysteine