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000859227 1001_ $$0P:(DE-Juel1)165994$$aKönig, Anna$$b0$$ufzj
000859227 245__ $$aHyperpolarized MAS NMR of unfolded and misfolded proteins
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000859227 520__ $$aIn this article we give an overview over the use of DNP-enhanced solid-state NMR spectroscopy for the investigation of unfolded, disordered and misfolded proteins. We first provide an overview over studies in which DNP spectroscopy has successfully been applied for the structural investigation of well-folded amyloid fibrils formed by short peptides as well as full-length proteins. Sample cooling to cryogenic temperatures often leads to severe line-broadening of resonance signals and thus a loss in resolution. However, inhomogeneous line-broadening at low temperatures provides valuable information about residual dynamics and flexibility in proteins, and, in combination with appropriate selective isotope labeling techniques, inhomogeneous line-widths in disordered proteins or protein regions may be exploited for evaluation of conformational ensembles. In the last paragraph we highlight some recent studies where DNP-enhanced MAS-NMR-spectroscopy was applied to the study of disordered proteins/protein regions and inhomogeneous sample preparations.
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000859227 7001_ $$0P:(DE-Juel1)165604$$aSchölzel, Daniel$$b1$$ufzj
000859227 7001_ $$0P:(DE-Juel1)161489$$aUluca, Boran$$b2$$ufzj
000859227 7001_ $$0P:(DE-Juel1)161253$$aViennet, Thibault$$b3
000859227 7001_ $$0P:(DE-Juel1)174523$$aAkbey, Ümit$$b4$$ufzj
000859227 7001_ $$0P:(DE-Juel1)132002$$aHeise, Henrike$$b5$$eCorresponding author$$ufzj
000859227 773__ $$0PERI:(DE-600)2021733-X$$a10.1016/j.ssnmr.2018.12.003$$gp. S0926204018300894$$p1-11$$tSolid state nuclear magnetic resonance$$v98$$x0926-2040$$y2019
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000859227 8767_ $$817991CV3$$92019-01-09$$d2019-01-09$$eHybrid-OA$$jZahlung erfolgt
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