Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: Protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy

D. Fushman, David Cowburn

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

We developed several approaches to direct determination of the 15N CSA from relaxation measurements in uniformly 15N-labeled proteins in solution. These methods are based on multiple-field measurements and could be extended to other nuclei in proteins and other molecules. Combined with the isotropic chemical shift measurements, this provides an experimental approach to full characterization of chemical shift tensors in proteins in their native milieu, which is likely to provide valuable information on the nature of chemical shifts and their relation to protein structure. Knowledge of 15N CSA is essential for an accurate characterization of protein dynamics from relaxation measurements.

Original languageEnglish (US)
Pages (from-to)109-126
Number of pages18
JournalMethods in Enzymology
Volume339
DOIs
StatePublished - 2001
Externally publishedYes

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Chemical shift
Tensors
Spectrum Analysis
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Spectroscopy
Proteins
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

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