TY - JOUR
T1 - 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
AU - Ortiz-Polo, Gilberto
AU - Krishnamoorthi, R.
AU - Markley, John L.
AU - Live, David H.
AU - Davis, Donald G.
AU - Cowburn, David
N1 - Funding Information:
This research was carried out, in part, at Purdue University, W. Lafayette, Indiana 47907, and was supported by U.S. Public Healtb Service Grants GM-19907 and RR-01077 (J.L.M.), GM-24267 (D.G.D.), and AM-20357 and RR-02434 (D.C.). D.C. thanks Professor A. G. Redfield for preprints of his studies.
PY - 1986/6/15
Y1 - 1986/6/15
N2 - 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 Peptide amide 1H NMR assignments obtained by two-dimensional 1H{1H} NMR methods (R. Krishnamoorthi and J. L. Markley, unpublished data) led to identification of the corresponding 1H{15N} MQ coherence cross peaks.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.
AB - 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 Peptide amide 1H NMR assignments obtained by two-dimensional 1H{1H} NMR methods (R. Krishnamoorthi and J. L. Markley, unpublished data) led to identification of the corresponding 1H{15N} MQ coherence cross peaks.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.
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U2 - 10.1016/0022-2364(86)90246-5
DO - 10.1016/0022-2364(86)90246-5
M3 - Article
AN - SCOPUS:46149130481
SN - 0022-2364
VL - 68
SP - 303
EP - 310
JO - Journal of Magnetic Resonance (1969)
JF - Journal of Magnetic Resonance (1969)
IS - 2
ER -