Journal Article

FZJ-2019-00108

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Hyperpolarized MAS NMR of unfolded and misfolded proteins

König, A.FZJ* ; Schölzel, D.FZJ* ; Uluca, B.FZJ* ; Viennet, T. ; Akbey, Ü.FZJ* ; Heise, H. (Corresponding author)FZJ*

2019
Elsevier Science [[-2000]] Amsterdam [u.a.]

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Please use a persistent id in citations: http://hdl.handle.net/2128/21350  doi:10.1016/j.ssnmr.2018.12.003

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2019

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Database coverage:
; ; ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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