A sensitive pulse scheme for measuring the backbone dihedral angle ψ based on cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation interactions

Daiwen Yang, Kevin H. Gardner, Lewis E. Kay

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

A pulse scheme for measuring cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle ψ is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring ψ based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and β-cyclodextrin.

Original languageEnglish (US)
Pages (from-to)213-220
Number of pages8
JournalJournal of Biomolecular NMR
Volume11
Issue number2
StatePublished - 1998

Fingerprint

Maltose-Binding Proteins
Anisotropy
Cyclodextrins
Chemical shift
Dihedral angle
Proteins

Keywords

  • Chemical shift anisotropy
  • Cross-correlation
  • Psi

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Spectroscopy

Cite this

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abstract = "A pulse scheme for measuring cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle ψ is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring ψ based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and β-cyclodextrin.",
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AU - Yang, Daiwen

AU - Gardner, Kevin H.

AU - Kay, Lewis E.

PY - 1998

Y1 - 1998

N2 - A pulse scheme for measuring cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle ψ is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring ψ based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and β-cyclodextrin.

AB - A pulse scheme for measuring cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle ψ is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring ψ based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and β-cyclodextrin.

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KW - Cross-correlation

KW - Psi

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