Enhanced spectral resolution in immobilized peptides and proteins by combining chemical shift sum and difference spectroscopy

Sorin Luca, Marc Baldus

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

A two-dimensional correlation experiment is introduced that records the sum and difference chemical shift of two scalar or dipolar coupled nuclei. Statistical results indicate that the suggested pulse scheme can significantly increase the possibility of separating chemical shift contributions due to residue type and backbone conformation in immobilized peptides and proteins. Experimental applications demonstrate the theoretical concept and lead to the predicted resolution enhancement between different amino acid types and among protein residues of different secondary structure.

Original languageEnglish (US)
Pages (from-to)243-249
Number of pages7
JournalJournal of Magnetic Resonance
Volume159
Issue number2
DOIs
StatePublished - Dec 1 2002

Fingerprint

Immobilized Proteins
Spectral resolution
Chemical shift
spectral resolution
peptides
chemical equilibrium
Spectrum Analysis
Spectroscopy
proteins
Amino Acids
Peptides
spectroscopy
amino acids
Conformations
Proteins
scalars
nuclei
augmentation
pulses
Experiments

Keywords

  • Chemical shifts
  • Correlation spectroscopy
  • Magic angle spinning
  • Protein backbone structure
  • Spectral resolution

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

Cite this

Enhanced spectral resolution in immobilized peptides and proteins by combining chemical shift sum and difference spectroscopy. / Luca, Sorin; Baldus, Marc.

In: Journal of Magnetic Resonance, Vol. 159, No. 2, 01.12.2002, p. 243-249.

Research output: Contribution to journalArticle

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