This title appears in the Scientific Report :
2019
Please use the identifier:
http://hdl.handle.net/2128/21350 in citations.
Please use the identifier: http://dx.doi.org/10.1016/j.ssnmr.2018.12.003 in citations.
Hyperpolarized MAS NMR of unfolded and misfolded proteins
Hyperpolarized MAS NMR of unfolded and misfolded proteins
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 we...
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Personal Name(s): | König, Anna |
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Schölzel, Daniel / Uluca, Boran / Viennet, Thibault / Akbey, Ümit / Heise, Henrike (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Solid state nuclear magnetic resonance, 98 (2019) S. 1-11 |
Imprint: |
Amsterdam [u.a.]
Elsevier Science [[-2000]]
2019
|
PubMed ID: |
30641444 |
DOI: |
10.1016/j.ssnmr.2018.12.003 |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Link: |
Get full text Get full text OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1016/j.ssnmr.2018.12.003 in citations.
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 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. |