Binding Site Identification and Structure Determination of ProteinLigand Complexes by NMR: A Semiautomated Approach

Joshua J. Ziarek, Francis C. Peterson, Betsy L. Lytle, Brian F. Volkman

Research output: Chapter in Book/Report/Conference proceedingChapter

61 Scopus citations

Abstract

Abstract Over the last 15 years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like compounds because of its ability to identify binding sites, affinities, and ligand poses at the level of individual amino acids without necessarily solving the structure of the proteinligand complex. However, it can also provide structures of flexible proteins and low-affinity (K d > 10 - 6 M) complexes, which often fail to crystallize. This chapter emphasizes a throughput-focused protocol that aims to identify practical aspects of binding site characterization, automated and semiautomated NMR assignment methods, and structure determination of proteinligand complexes by NMR.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc
Pages241-275
Number of pages35
DOIs
StatePublished - 2011

Publication series

NameMethods in Enzymology
Volume493
ISSN (Print)0076-6879

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Binding Site Identification and Structure Determination of ProteinLigand Complexes by NMR: A Semiautomated Approach'. Together they form a unique fingerprint.

Cite this