Exotic Protein NMR

  • Tertiary and Quaternary Structure. Aggregation State
  • Modular Proteins ( 04CR3557 )
  • Unfolded proteins, Denatured Proteins, NMR in disordered states
  • Encapsulated Proteins studied by NMR ( 01METH54-338 , 03JB313-25 and 02JB311 )
  • 19F NMR in fluorine-containing proteins
  • High-pressure NMR of proteins ( 01METH134-338 ). Use of dipolar couplings ( 01JB173-21 ).
  • In-cell NMR Spectroscopy ( 05METH17 ).
  • Miscellaneous

  • Simultaneous 3D HNCO/HNCA for 15N labeled proteins with 13C at natural abundance ( 03JB175-27 )
  • NMR Biomolecular Sample conditions:
  • Physiological conditions and practicality for protein NMR ( 01METH3-339 )
  • Optimization of protein solubility and stability for protein NMR ( 01METH20-339 )
  • pKa measurements: Side-chain carboxyl pKa values of Asp and Glu moieties provide important information on the electrostatic environment of these residues:
  • pH dependence of side-chain carboxyl carbon or proton chemical shifts in folded proteins ( 01BIO10115 and 96BIO9945 )
  • Measurement in unfolded protein ( 02JACS5714 )
  • Example in 98BIO15865
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