期刊
SOLID STATE NUCLEAR MAGNETIC RESONANCE
卷 98, 期 -, 页码 1-11出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ssnmr.2018.12.003
关键词
Dynamic nuclear polarization; Intrinsically disordered proteins; Amyloid fibrils; Conformational ensemble; Frozen solution; Solid-state NMR
资金
- DFG [HE 3243/4-1]
- Ministry of Innovation, Science and Research
- International Graduate School of Protein Science and Technology (iGRASPseed) by the Ministry of Innovation, Science and Research of the state North Rhine-Westphalia
In 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 linewidths 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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