2012
DOI: 10.1016/j.jsb.2012.08.008
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Quantitative analysis of spin exchange interactions to identify β strand and turn regions in Ure2 prion domain fibrils with site-directed spin labeling

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Cited by 17 publications
(37 citation statements)
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“…Confirmation of this result for Ure2p comes from analogous experiments using electron spin resonance instead of NMR (118). Such experiments also suggest the locations of some of the folds (119).…”
Section: Het-s Infectious Amyloid Is a ␤-Helixsupporting
confidence: 53%
“…Confirmation of this result for Ure2p comes from analogous experiments using electron spin resonance instead of NMR (118). Such experiments also suggest the locations of some of the folds (119).…”
Section: Het-s Infectious Amyloid Is a ␤-Helixsupporting
confidence: 53%
“…The EPR sample can be in solutions, aggregates, or membrane environments, and of any size. As shown previously in the studies of A␤ and yeast prion protein Ure2p, EPR can resolve structural heterogeneity and separate different structural states (23)(24)(25)(26). Distance measurements with continuous-wave and pulsed EPR can cover a wide range of distances from 5 to 70 Å (27,28).…”
mentioning
confidence: 77%
“…Strong spin exchange interactions lead to the collapse of the three-line EPR spectrum, which is typical of a nitroxide spin label, to a single-line spectrum, providing a signature for the parallel in-register β-sheet structure (Agopian and Guo, 2012; Chen et al, 2007; Ngo et al, 2011; Török et al, 2002). Previous work shows that quantitative analysis of the spin exchange interaction can identify the location of β-strands and turns (Ngo et al, 2012). The rationale is that the side chain stacking of introduced spin labels leading to the single-line EPR spectrum requires the residue to be located on well-ordered β-strands.…”
Section: Introductionmentioning
confidence: 99%
“…The rationale is that the side chain stacking of introduced spin labels leading to the single-line EPR spectrum requires the residue to be located on well-ordered β-strands. In general, turns are not as ordered as β-strands, and thus spin labels located on the turn would have much weaker spin-spin interactions than a β-strand site (Ngo et al, 2012). …”
Section: Introductionmentioning
confidence: 99%