13C NMR chemical shifts can predict disulfide bond formation

Research output: Contribution to journalArticle

202 Citations (Scopus)

Abstract

The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded) state. A database of cysteine 13C C(α) and C(β) chemical shifts was constructed from the BMRB and Sheffield databases, and published journals. Statistical analysis indicated that the C(β) shift is extremely sensitive to the redox state, and can predict the disulfide-bonded state. Further, chemical shifts in both states occupy distinct clusters as a function of secondary structure in the C(α)/C(β) chemical shift map. On the basis of these results, we provide simple ground rules for predicting the redox state of cysteines; these rules could be used effectively in NMR structure determination, predicting new folds, and in protein folding studies.

Original languageEnglish (US)
Pages (from-to)165-171
Number of pages7
JournalJournal of Biomolecular NMR
Volume18
Issue number2
DOIs
StatePublished - 2000

Fingerprint

Chemical shift
Disulfides
Nuclear magnetic resonance
Cysteine
Oxidation-Reduction
Databases
Protein folding
X ray crystallography
X Ray Crystallography
Protein Folding
Statistical methods
Carbon-13 Magnetic Resonance Spectroscopy

Keywords

  • C
  • Chemical shifts
  • Cysteine
  • Disulfide bond
  • Redox

ASJC Scopus subject areas

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

Cite this

13C NMR chemical shifts can predict disulfide bond formation. / Sharma, D.; Rajarathnam, Krishna.

In: Journal of Biomolecular NMR, Vol. 18, No. 2, 2000, p. 165-171.

Research output: Contribution to journalArticle

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AB - The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded) state. A database of cysteine 13C C(α) and C(β) chemical shifts was constructed from the BMRB and Sheffield databases, and published journals. Statistical analysis indicated that the C(β) shift is extremely sensitive to the redox state, and can predict the disulfide-bonded state. Further, chemical shifts in both states occupy distinct clusters as a function of secondary structure in the C(α)/C(β) chemical shift map. On the basis of these results, we provide simple ground rules for predicting the redox state of cysteines; these rules could be used effectively in NMR structure determination, predicting new folds, and in protein folding studies.

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