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Deuterated peptides and proteins: Structure and dynamics studies by MAS solid-state NMR.

Methods Mol. Biol. 831, 279-301 (2012)
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Perdeuteration and back substitution of exchangeable protons in microcrystalline proteins, in combination with recrystallization from D(2)O-containing buffers, significantly reduce (1)H, (1)H dipolar interactions. This way, amide proton line widths on the order of 20 Hz are obtained. Aliphatic protons are accessible either via specifically protonated precursors or by using low amounts of H(2)O in the bacterial growth medium. The labeling scheme enables characterization of structure and dynamics in the solid-state without dipolar truncation artifacts.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Herausgeber Shekhtman, A.* ; Burz, D.S.*
Schlagwörter 15n Relaxation ; 2h Labeling ; Magic Angle Spinning Solid-state Nmr ; Microcrystalline Proteins ; Order Parameters ; Perdeuteration ; Protein Dynamics
ISSN (print) / ISBN 1064-3745
e-ISSN 1940-6029
Konferenztitel Protein NMR Techniques
Quellenangaben Band: 831, Heft: , Seiten: 279-301 Artikelnummer: , Supplement: ,
Verlag Springer
Verlagsort Berlin [u.a.]
Begutachtungsstatus Peer reviewed