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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.