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Open Access Green as soon as Postprint is submitted to ZB.
Deuterated peptides and proteins: Structure and dynamics studies by MAS solid-state NMR.
Methods Mol. Biol. 831, 279-301 (2012)
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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Publication type
Article: Journal article
Document type
Scientific Article
Editors
Shekhtman, A.* ; Burz, D.S.*
Keywords
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
Conference Title
Protein NMR Techniques
Journal
Methods in Molecular Biology
Quellenangaben
Volume: 831,
Pages: 279-301
Publisher
Springer
Publishing Place
Berlin [u.a.]
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)