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Linser, R.* ; Fink, U.* ; Reif, B.*

Assignment of dynamic regions in biological solids enabled by spin-state selective NMR experiments.

J. Am. Chem. Soc. 132, 8891-8893 (2010)
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Structural investigations are a prerequisite to understand protein function. Intermediate time scale motional processes (ns-micros) are deleterious for NMR of biological solids and obscure the detection of amide moieties in traditional CP based solid-state NMR approaches as well as in regular scalar coupling based experiments. We show that this obstacle can be overcome by using TROSY type techniques in triple resonance experiments, which enable the assignment of resonances in loop regions of a microcrystalline protein. The presented approach provides an exemplified solution for the analysis of secondary structure elements undergoing slow dynamics that might be particularly crucial for understanding protein function.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
ISSN (print) / ISBN 0002-7863
e-ISSN 1520-5126
Quellenangaben Band: 132, Heft: 26, Seiten: 8891-8893 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Begutachtungsstatus Peer reviewed