TY - JOUR
T1 - Characterization of dynamics of perdeuterated proteins by MAS solid-state NMR
AU - Hologne, Maggy
AU - Faelber, Katja
AU - Diehl, Anne
AU - Reif, Bernd
PY - 2005/8/17
Y1 - 2005/8/17
N2 - We show in this communication that dynamic information for uniformly 2H,13C,15N isotopically enriched, crystalline proteins can be obtained by MAS solid-state NMR spectroscopy. The experiments make use of the deuterium quadrupolar tensor, which is the dominant interaction mechanism. Dynamic properties are accessed by measurement of the size of the quadrupolar coupling constant, Cq, and the value of the asymmetry parameter, η, via evolution of the deuterium chemical shift, as well as by measurement of deuterium T1 relaxation times. Three-dimensional experiments are performed in order to obtain site-specific resolution. Due to proton dilution, no proton decoupling is required in the carbon evolution periods at MAS rotation frequencies of 10 kHz.
AB - We show in this communication that dynamic information for uniformly 2H,13C,15N isotopically enriched, crystalline proteins can be obtained by MAS solid-state NMR spectroscopy. The experiments make use of the deuterium quadrupolar tensor, which is the dominant interaction mechanism. Dynamic properties are accessed by measurement of the size of the quadrupolar coupling constant, Cq, and the value of the asymmetry parameter, η, via evolution of the deuterium chemical shift, as well as by measurement of deuterium T1 relaxation times. Three-dimensional experiments are performed in order to obtain site-specific resolution. Due to proton dilution, no proton decoupling is required in the carbon evolution periods at MAS rotation frequencies of 10 kHz.
UR - http://www.scopus.com/inward/record.url?scp=23844490048&partnerID=8YFLogxK
U2 - 10.1021/ja051830l
DO - 10.1021/ja051830l
M3 - Article
C2 - 16089426
AN - SCOPUS:23844490048
SN - 0002-7863
VL - 127
SP - 11208
EP - 11209
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 32
ER -