Detection of nuclear overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy

Journal Article · Tue Nov 20 23:00:00 EST 1990 · Journal of the American Chemical Society; (United States)

DOI:https://doi.org/10.1021/ja00180a080· OSTI ID:5233916

Ikura, Mitsuhiko; Bax, A; Clore, G M; Gronenborn, A M ^[1]

---

1. National Inst. of Diabetes and Digestive and Kidney Diseases, Bethesda, MD (USA)

The key to protein structure determination by NMR lies in the identification of as many {sup 1}H-{sup 1}H nuclear Overhauser effects (NOEs) as possible in order to obtain a large set of approximate interproton distance restraints. With the advent of a range of heteronuclear three-dimensional (3D) NMR experiments, it has now become possible to obtain complete {sup 1}H, {sup 15}N, and {sup 13}C assignments and to determine the 3D structures of proteins in the 15-25-kDa molecular weight range. Despite these advances, it has remained impossible to observe NOEs between protons with degenerate chemical shifts. Such interactions occur repeatedly, both among aliphatic or aromatic protons and between sequential amide protons in helical proteins. Here the authors describe a 3D heteronuclear experiment that allows the observation of these NOEs and demonstrate its applicability for calmodulin, a protein of 148 residues and molecular weight 16.7 kDa.

• OSTI ID: 5233916
• Journal Information: Journal of the American Chemical Society; (United States), Journal Name: Journal of the American Chemical Society; (United States) Vol. 112:24; ISSN 0002-7863; ISSN JACSA
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400201* -- Chemical & Physicochemical Properties
550200 -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMISTRY
CALMODULIN
CHEMISTRY
DATA
EXPERIMENTAL DATA
INFORMATION
MAGNETIC RESONANCE
MEASURING METHODS
NUCLEAR MAGNETIC RESONANCE
NUMERICAL DATA
ORGANIC COMPOUNDS
PROTEIN STRUCTURE
PROTEINS
RESONANCE