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Solid state NMR studies of ligand dynamics and conformations is the binding sites of the gastric H+/K+-ATPase

Solid state NMR studies of ligand dynamics and conformations is the binding sites of the gastric H+/K+-ATPase

Detalhes bibliográficos
Main Authors: Watts, J, Watts, A, Middleton, D
Formato: Journal article
Publicado em: 2000
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Registos relacionados

  • Solid state NMR studies of ligand conformations in the binding sites of ion translocating APTases
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  • A model of reversible inhibitors in the gastric H+/K+-ATPase binding site determined by rotational echo double resonance NMR.
    Por: Watts, J, et al.
    Publicado em: (2001)
  • Ligand docking in the gastric H+/K+-ATPase: homology modeling of reversible inhibitor binding sites.
    Por: Kim, C, et al.
    Publicado em: (2005)
  • The conformations of a functional spin-labeled derivative of gastric H/K-ATPase investigated by EPR spectroscopy.
    Por: Middleton, D, et al.
    Publicado em: (1995)
  • Structural descriptions of ligands in their binding site of integral membrane proteins at near physiological conditions using solid-state NMR
    Por: Watts, A, et al.
    Publicado em: (1998)

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