67Zn solid-state NMR spectroscopy of the minimal dna binding domain of human nucleotide excision repair protein XPA.
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Biomedical subjects
Publications and source records attributed to J A Sears.
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A general strategy for the observation of low gamma half-integer quadrupolar nuclides in biological systems is presented. The methodology combines low-temperature (4-100 K) techniques with cross-polarization (CP) experiments while employing a so-called Carr-Purcell-Meiboom-Gill spin-echo sequence (CPMG). This combined approach is termed CP/QCPMG. Also discussed are data processing issues that are unique to the induced signals that result from the QCPMG pulse sequence. Central to this strategy is the development of a stable low-temperature (4 to 250 K) NMR double-resonance probe. The probe is robust enough to handle multiple contact experiments and long acquisition periods with 1H decoupling. This approach is illustrated with low-temperature solid-state 67Zn and 25Mg NMR CP/QCPMG experiments on model compounds. The conclusion reached is that the strategy affords sufficient sensitivity to examine Zn2+ and/or Mg2+ binding sites in metalloproteins.
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