title: Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers.
abstract: For micro-crystalline proteins, solid-state nuclear magnetic resonance spectroscopy of perdeuterated samples can provide spectra of unprecedented quality. Apart from allowing to detect sparsely introduced protons and thereby increasing the effective resolution for a series of sophisticated techniques, deuteration can provide extraordinary coherence lifetimes--obtainable for all involved nuclei virtually without decoupling and enabling the use of scalar magnetization transfers. Unfortunately, for fibrillar or membrane-embedded proteins, significantly shorter transverse relaxation times have been encountered as compared to micro-crystalline proteins despite an identical sample preparation, calling for alternative strategies for resonance assignment. In this work we propose an approach towards sequential assignment of perdeuterated proteins based on long-range (1)H/(13)C Cross Polarization transfers. This strategy gives rise to H/N-separated correlations involving C(α), C(β), and CO chemical shifts of both, intra- and interresidual contacts, and thus connecting adjacent residues independent of transverse relaxation times.
authors.affiliation: Analytical Centre, University of New South Wales, Sydney, NSW, 2052, Australia. rasmus_linser@hms.harvard.edu
authors.forename: Rasmus
authors.initials: R
authors.lastname: Linser
mesh_terms: D000818:Animals; D002645:Chickens; D003903:Deuterium / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D013049:Spectrin / Q000737:chemistry
chemical_list: D011506:Proteins; D011522:Protons; D013049:Spectrin; D003903:Deuterium