STD NMR as a Technique for Ligand Screening and Structural Studies

Samuel Walpole, Serena Monaco, Ridvan Nepravishta, Jesus Angulo (Lead Author)

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

15 Citations (Scopus)

Abstract

STD NMR is a powerful ligand-based tool for screening small molecules and low molecular weight fragments for their interaction with a given macromolecule. Such information is invaluable both in the drug discovery sector and in understanding fundamental biological interactions. Recently, powerful methods have been developed to extract a greater wealth of information from the STD NMR experiment, including ligand binding epitopes, dissociation constant determination, and mapping of binding site properties. Herein we describe these STD NMR experiments, giving practical examples for each approach, and highlight the important parameters and common pitfalls that must be considered for a successful experiment.
Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherElsevier
Chapter12
Pages423-451
Number of pages29
Volume608
DOIs
Publication statusPublished - 2019

Keywords

  • Saturation transfer difference NMR
  • STD NMR
  • Protein–ligand interactions
  • Ligand screening
  • DEEP-STD NMR
  • Binding epitope mapping

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