A refocused and optimized HNCA: increased sensitivity and resolution in large macromolecules

A 3D optimized, refocused HNCA experiment is described. It is demonstrated to yield a dramatic increase in sensitivity when applied to [13C, 15N]-labeled human carbonic anhydrase II, a 29-kDa protein. The reasons for the gain in sensitivity are discussed, and 3 distinct areas for further development...

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Bibliographic Details
Published in:Journal of biomolecular NMR 1992-03, Vol.2 (2), p.195-202
Main Authors: Farmer, 2nd, B T, Venters, R A, Spicer, L D, Wittekind, M G, Müller, L
Format: Article
Language:English
Subjects:
Carbon Isotopes
Carbonic Anhydrases - chemistry
Humans
Isoenzymes - chemistry
Magnetic Resonance Spectroscopy - methods
Mathematics
Nitrogen Isotopes
Protein Conformation
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Summary:A 3D optimized, refocused HNCA experiment is described. It is demonstrated to yield a dramatic increase in sensitivity when applied to [13C, 15N]-labeled human carbonic anhydrase II, a 29-kDa protein. The reasons for the gain in sensitivity are discussed, and 3 distinct areas for further development are indicated.
ISSN:0925-2738
1573-5001
DOI:10.1007/bf01875530