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Isotope-Coded Affinity Tags with Tunable Reactivities for Protein Footprinting
Angewandte Chemie (2008)
  • Eric S. Underbakke, University of Wisconsin - Madison
  • Yimin Zhu, University of Wisconsin - Madison
  • Laura L. Kiessling, University of Wisconsin - Madison
Fundamental to our understanding of biological systems is the ability to define interaction surfaces and conformational changes in dynamic protein complexes, yet this objective remains a challenge. Protein footprinting is a powerful solution to this problem. Methods such as hydrogen-deuterium exchange[1] limited proteolysis,[2] and radiolytic cleavage[3] assess changes in protein surface exposure by measuring the susceptibility of the polypeptide backbone to modification. A complementary approach is to use side-chain modification. Because of their unique nucleophilicity, cysteine (Cys) residues at select positions can report
on solvent accessibility and local chemical environment.[4] The reactivity of a Cys residue can be measured to define interaction surfaces at individual amino acid resolution. Moreover, methods have been developed for rapid generation of a library of Cys variants for a protein of interest.
  • alkylation,
  • footprinting,
  • isotope-coded affinity tag,
  • mass spectrometry,
  • protein modification
Publication Date
Publisher Statement
This is the peer reviewed version of the following article: Underbakke, Eric S., Zhu, Y. and Kiessling, Laura L. (2008), Isotope-Coded Affinity Tags with Tunable Reactivities for Protein Footprinting. Angewandte Chemie, 120: 9823–9826, which has been published in final form at doi:10.1002/ange.200803378. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving
Citation Information
Eric S. Underbakke, Yimin Zhu and Laura L. Kiessling. "Isotope-Coded Affinity Tags with Tunable Reactivities for Protein Footprinting" Angewandte Chemie Vol. 47 Iss. 50 (2008) p. 9677 - 9680
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