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@ARTICLE{Knig:859227,
author = {König, Anna and Schölzel, Daniel and Uluca, Boran and
Viennet, Thibault and Akbey, Ümit and Heise, Henrike},
title = {{H}yperpolarized {MAS} {NMR} of unfolded and misfolded
proteins},
journal = {Solid state nuclear magnetic resonance},
volume = {98},
issn = {0926-2040},
address = {Amsterdam [u.a.]},
publisher = {Elsevier Science [[-2000]]},
reportid = {FZJ-2019-00108},
pages = {1-11},
year = {2019},
abstract = {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.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:30641444},
UT = {WOS:000458528900001},
doi = {10.1016/j.ssnmr.2018.12.003},
url = {https://juser.fz-juelich.de/record/859227},
}