OpenSSL SSL_connect: Connection reset by peer in connection to v2.sherpa.ac.uk:443 PuSH - Publication Server of Helmholtz Zentrum München: Deuterated peptides and proteins: Structure and dynamics studies by MAS solid-state NMR.

PuSH - Publication Server of Helmholtz Zentrum München

Reif, B.

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

Methods Mol. Biol. 831, 279-301 (2012)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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.*
Corresponding Author
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, Issue: , Pages: 279-301 Article Number: , Supplement: ,
Publisher Springer
Publishing Place Berlin [u.a.]
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)