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

Journal Article · Wed Feb 07 00:00:00 EST 2001 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/ja003720e· OSTI ID:15002191

Lipton, Andrew S ^[1]; Buchko, Garry W ^[1]; Sears, Jesse A ^[1]; Kennedy, Michael A ^[1]; Ellis, Paul D ^[1]

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1. BATTELLE (PACIFIC NW LAB)

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.

• Research Organization: Pacific Northwest National Lab., Richland, WA (US)
• Sponsoring Organization: US Department of Energy (US)
• DOE Contract Number: AC06-76RL01830
• OSTI ID: 15002191
• Report Number(s): PNWD-SA-5156; TRN: US200408%%158
• Journal Information: Journal of the American Chemical Society, Vol. 123, Issue 5; Other Information: PBD: 7 Feb 2001
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
CHEMICAL SHIFT
DNA
EXCISION REPAIR
MAGNETS
METALLOPROTEINS
NUCLEOTIDES
PROTEINS
QUADRUPOLES
RELAXATION
SPECTROSCOPY
ZINC