TY - CHAP
T1 - Deuterated peptides and proteins
T2 - Structure and dynamics studies by MAS solid-state NMR
AU - Reif, Bernd
PY - 2012
Y1 - 2012
N2 - Perdeuteration and back substitution of exchangeable protons in microcrystalline proteins, in combination with recrystallization from D 2O-containing buffers, significantly reduce 1H, 1H 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 H2O in the bacterial growth medium. The labeling scheme enables characterization of structure and dynamics in the solid-state without dipolar truncation artifacts.
AB - Perdeuteration and back substitution of exchangeable protons in microcrystalline proteins, in combination with recrystallization from D 2O-containing buffers, significantly reduce 1H, 1H 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 H2O in the bacterial growth medium. The labeling scheme enables characterization of structure and dynamics in the solid-state without dipolar truncation artifacts.
KW - H labeling
KW - Magic angle spinning solid-state NMR
KW - Microcrystalline proteins
KW - N relaxation
KW - Order parameters
KW - Perdeuteration
KW - Protein dynamics
UR - http://www.scopus.com/inward/record.url?scp=84855888946&partnerID=8YFLogxK
U2 - 10.1007/978-1-61779-480-3_16
DO - 10.1007/978-1-61779-480-3_16
M3 - Chapter
C2 - 22167680
AN - SCOPUS:84855888946
SN - 9781617794797
T3 - Methods in Molecular Biology
SP - 279
EP - 301
BT - Protein NMR Techniques
ER -