The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins

Kevin H. Gardner, Lewis E. Kay

Research output: Contribution to journalArticle

465 Citations (Scopus)

Abstract

During the past thirty years, deuterium labeling has been used to improve the resolution and sensitivity of protein NMR spectra used in a wide variety of applications. Most recently, the combination of triple resonance experiments and 2H, 13C, 15N labeled samples has been critical to the solution structure determination of several proteins with molecular weights on the order of 30 kDa. Here we review the developments in isotopic labeling strategies, NMR pulse sequences, and structure-determination protocols that have facilitated this advance and hold promise for future NMR-based structural studies of even larger systems. As well, we detail recent progress in the use of solution 2H NMR methods to probe the dynamics of protein sidechains.

Original languageEnglish (US)
Pages (from-to)357-406
Number of pages50
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume27
DOIs
StatePublished - 1998

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Nuclear magnetic resonance
Proteins
Labeling
Deuterium
Sequence Analysis
Molecular Weight
Molecular weight
Experiments

Keywords

  • Amino acid-specific isotopic labeling
  • Protein deuteration
  • Sidechain dynamics
  • Structure determination
  • Triple resonance NMR

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

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KW - Protein deuteration

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