Triple resonance experiments are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, most typically consisting of 1H, 15N and 13C. These experiments are often used to assign specific resonance signals to specific atoms in an isotopically-enriched protein. The technique was first described in papers by Ad Bax, Mitsuhiko Ikura and Lewis Kay in 1990, and further experiments were then added to the suite of experiments. Many of these experiments have since become the standard set of experiments used for sequential assignment of NMR resonances in the determination of protein structure by NMR. They are now an integral part of solution NMR study of proteins, and they may also be used in solid-state NMR.
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| - Triple-resonance nuclear magnetic resonance spectroscopy (en)
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| - Triple resonance experiments are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, most typically consisting of 1H, 15N and 13C. These experiments are often used to assign specific resonance signals to specific atoms in an isotopically-enriched protein. The technique was first described in papers by Ad Bax, Mitsuhiko Ikura and Lewis Kay in 1990, and further experiments were then added to the suite of experiments. Many of these experiments have since become the standard set of experiments used for sequential assignment of NMR resonances in the determination of protein structure by NMR. They are now an integral part of solution NMR study of proteins, and they may also be used in solid-state NMR. (en)
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| - The top and bottom figures show the magnetization transfer pathway with the atoms that appear as peaks highlighted. The middle figure shows how the peaks appear in spectra, here presented as an overlay of strips of HNCACB and CBCANH spectra. Peaks from CBCANH are in intensity plot and colored yellow; they identify the resonances of the preceding Cα and Cβ. HNCACB is in contour plot and usually shows 4 peaks for each strip, two each from a residue and its preceding one. The red peaks are for Cα, and blue peaks for Cβ. Here the blue Cβ peaks of threonine and alanine are distinctive and easily identifiable, while glycine which lacks a Cβ gives only a single peak. Other residue types however may not be as easy to distinguish. (en)
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| - Sequential assignment using triple resonance experiments (en)
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| - CBCACONH experiment.JPG (en)
- HNCACB experiment.JPG (en)
- NMR sequential assignment strips.JPG (en)
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| - Triple resonance experiments are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, most typically consisting of 1H, 15N and 13C. These experiments are often used to assign specific resonance signals to specific atoms in an isotopically-enriched protein. The technique was first described in papers by Ad Bax, Mitsuhiko Ikura and Lewis Kay in 1990, and further experiments were then added to the suite of experiments. Many of these experiments have since become the standard set of experiments used for sequential assignment of NMR resonances in the determination of protein structure by NMR. They are now an integral part of solution NMR study of proteins, and they may also be used in solid-state NMR. (en)
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