Description

Significance: 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

Significance: 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. Recent Advances: Many different molecular probes are now commercially available to label and track cysteine residues at great sensitivity.

application/pdf

Download count: 0

Details

Contributors
Date Created
  • 2014-07-20
Resource Type
  • Text
  • Collections this item is in
    Identifier
    • Digital object identifier: 10.1089/ars.2013.5559
    • Identifier Type
      International standard serial number
      Identifier Value
      1523-0864
    • Identifier Type
      International standard serial number
      Identifier Value
      1557-7716
    Note

    Citation and reuse

    Cite this item

    This is a suggested citation. Consult the appropriate style guide for specific citation guidelines.

    Borges, Chad R., & Sherma, Nisha D. (2014). Techniques for the Analysis of Cysteine Sulfhydryls and Oxidative Protein Folding. ANTIOXIDANTS & REDOX SIGNALING, 21(3), 511-531. http://dx.doi.org/10.1089/ars.2013.5559

    Machine-readable links