Resolution and measurement of heteronuclear dipolar couplings of a noncrystalline protein immobilized in a biological supramolecular assembly by proton-detected MAS solid-state NMR spectroscopy

Two-dimensional (15)N chemical shift/(1)H chemical shift and three-dimensional (1)H-(15)N dipolar coupling(/15)N chemical shift/(1)H chemical shift MAS solid-state NMR correlation spectra of the filamentous bacteriophage Pf1 major coat protein show single-site resolution in noncrystalline, intact-ph...

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Bibliographische Detailangaben
Hauptverfasser: Park, Sang Ho, Yang, Chen, Opella, Stanley J., Mueller, Leonard J.
Format: Artigo
Sprache:Inglês
Veröffentlicht: 2013
Schlagworte:
Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3915937/
https://ncbi.nlm.nih.gov/pubmed/24225529
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmr.2013.10.009
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