Determination of slow motions in extensively isotopically labeled proteins by magic-angle-spinning 13C-detected 15N exchange NMR

Autor:	E.R. deAzevedo, S. B. Kennedy, Mei Hong
Rok vydání:	2000
Předmět:	chemistry.chemical_compound Magnetization Millisecond Nuclear magnetic resonance chemistry Solid-state nuclear magnetic resonance Carbon-13 NMR satellite Amide Magic angle spinning General Physics and Astronomy High resolution Physical and Theoretical Chemistry Anisotropy
Zdroj:	Chemical Physics Letters. 321:43-48
ISSN:	0009-2614
Popis:	A solid-state NMR exchange technique for detecting slow segmental dynamics in proteins is introduced. The technique exploits motion-induced incomplete refocusing of amide 15 N chemical shift anisotropy under magic angle spinning. Slow motions on the millisecond timescales are detected as reduced NMR signals. Detection of 13 C magnetization transferred from 15 N allows the identification of mobile residues with high resolution. This exchange technique is demonstrated on two proteins with opposite motional properties. Combined with extensive 13 C and 15 N labeling, this high-resolution exchange NMR technique allows for the first time the efficient determination of slow dynamics at multiple residues of proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::ba441f8c48e8b85a465d6b127ac5c346 https://doi.org/10.1016/s0009-2614(00)00310-9 Zobrazit plný text záznamu Full Text from ScienceDirect