High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy.
A highly sensitive new 1H-detected 3D solid-state NMR method is described for characterizing 1H-1H spin exchange in nanocrystalline samples of 15N- and 2H-enriched protein. Long-range contacts are observed in human ubiquitin. The method is also used to show that numerous NOEs between backbone amides and crystal water protons can be observed.
Paulson
Eric K
EK
Department of Chemistry, Yale University, P.O. Box 208107, New Haven, CT 06520-8107, USA.
Morcombe
Corey R
CR
Gaponenko
Vadim
V
Dancheck
Barbara
B
Byrd
R Andrew
RA
Zilm
Kurt W
KW
D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017433:Protein Structure, Secondary; D011522:Protons; D012680:Sensitivity and Specificity; D025801:Ubiquitin / Q000737:chemistry*
D011522:Protons; D025801:Ubiquitin