Natural-abundance 15N NMR studies of Turkey ovomucoid third domain. Assignment of peptide 15N resonances to the residues at the reactive site region via proton-detected multiple-quantum coherence

Gilberto Ortiz-Polo, R. Krishnamoorthi, John L. Markley, David H. Live, Donald G. Davis, David Cowburn

Research output: Contribution to journalArticle

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Abstract

Heteronuclear two-dimensional 1H{15N} multiple-quantum (MQ) spectroscopy has been applied to a protein sample at natural abundance: ovomucoid third domain from turkey (Meleagris gallopavo), a serine proteinase inhibitor of 56 amino acid residues. Peptide amide 1H NMR assignments obtained by two-dimensional 1H{1H} NMR methods (R. Krishnamoorthi and J. L. Markley, unpublished data) led to identification of the corresponding 1H{15N} MQ coherence cross peaks. From these, 15N NMR chemical shifts were determined for several specific backbone amide groups of amino acid residues located around the reactive site region of the inhibitor. The results suggest that amide 15N chemical shifts, which are readily obtained in this way, may serve as sensitive probes for conformational studies of proteins.

Original languageEnglish (US)
Pages (from-to)303-310
Number of pages8
JournalJournal of Magnetic Resonance (1969)
Volume68
Issue number2
DOIs
StatePublished - Jun 15 1986
Externally publishedYes

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Ovomucin
Amides
Protons
Nuclear magnetic resonance
Chemical shift
Peptides
Amino Acids
Serine Proteinase Inhibitors
Proteins
Spectroscopy

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Natural-abundance 15N NMR studies of Turkey ovomucoid third domain. Assignment of peptide 15N resonances to the residues at the reactive site region via proton-detected multiple-quantum coherence. / Ortiz-Polo, Gilberto; Krishnamoorthi, R.; Markley, John L.; Live, David H.; Davis, Donald G.; Cowburn, David.

In: Journal of Magnetic Resonance (1969), Vol. 68, No. 2, 15.06.1986, p. 303-310.

Research output: Contribution to journalArticle

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AU - Cowburn, David

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