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2000
Volume 11, Issue 4
  • ISSN: 1389-5575
  • E-ISSN: 1875-5607

Abstract

In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.

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/content/journals/mrmc/10.2174/138955711795305344
2011-04-01
2025-10-02
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