title: High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy.
abstract: 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.
authors: Department of Chemistry, Yale University, P.O. Box 208107, New Haven, CT 06520-8107, USA.
authors: Eric K
authors: EK
authors: Paulson
authors: Corey R
authors: CR
authors: Morcombe
authors: Vadim
authors: V
authors: Gaponenko
authors: Barbara
authors: B
authors: Dancheck
authors: R Andrew
authors: RA
authors: Byrd
authors: Kurt W
authors: KW
authors: Zilm
mesh_terms: 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*
chemical_list: D011522:Protons; D025801:Ubiquitin