Zn-67 Solid-State NMR Spectroscopy of the Minimal DNA Binding Domain of Human Nucleotide Excision Repair Protein XPA

February 7, 2001

Journal Article

Zn-67 Solid-State NMR Spectroscopy of the Minimal DNA Binding Domain of Human Nucleotide Excision Repair Protein XPA

Abstract

Historically it has not been possible to directly observe the native zinc metal of Zn2+ metalloproteins by liquid- or solid-state NMR methods. Even with today's 21 T magnets, it solution NMR methods afforded observable resonances in a metalloprotein, the resulting linewidths (due quadrupole relaxation) would be such as to obscure the determination of site specific isotropic chemical shifts.

Revised: January 17, 2011 | Published: February 7, 2001

Citation

Lipton A.S., G.W. Buchko, J.A. Sears, M.A. Kennedy, and P.D. Ellis. 2001. Zn-67 Solid-State NMR Spectroscopy of the Minimal DNA Binding Domain of Human Nucleotide Excision Repair Protein XPA. Journal of the American Chemical Society 123, no. 5:992-993. PNWD-SA-5156.