Constant-time through-bond 13C correlation spectroscopy for assigning protein resonances with solid-state NMR spectroscopy.
Even as available magnetic fields for NMR continue to increase, resolution remains one of the most critical limitations in assigning and solving structures of larger biomolecules. Here we present a novel constant-time through-bond correlation spectroscopy for solids that offers superior resolution for 13C chemical shift assignments in proteins. In this experiment, the indirect evolution and transfer periods are combined into a single constant time interval, offering increased resolution while not sacrificing sensitivity. In GB1, this allows us to resolve peaks that are otherwise unresolved and to make assignments in the absence of multibond transfers.
Chen
Lingling
L
Department of Chemistry, University of California, Riverside, California 92521, USA.
Olsen
Ryan A
RA
Elliott
Douglas W
DW
Boettcher
John M
JM
Zhou
Donghua H
DH
Rienstra
Chad M
CM
Mueller
Leonard J
LJ
D002247:Carbon Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
D002247:Carbon Isotopes; D011506:Proteins