NDLI: $^{13}$C, $^{15}$N Resonance Assignment of Parts of the HET-s Prion Protein in its Amyloid Form

Content Provider	Springer Nature Link
Author	Siemer, Ansgar B. Ritter, Christiane Steinmetz, Michel O. Ernst, Matthias Riek, Roland Meier, Beat H.
Copyright Year	2006
Abstract	The partial $^{15}$N and $^{13}$C solid-state NMR resonance assignment of the HET-s prion protein fragment 218–289 in its amyloid form is presented. It is based on experiments measured at MAS frequencies in the range of 20–40 kHz using exclusively adiabatic polarization-transfer schemes. The resonance assignment within each residue is based on two-dimensional $^{13}$C––$^{13}$C correlation spectra utilizing the DREAM mixing scheme. The sequential linking of the assigned residues used a set of two- and three-dimensional $^{15}$N––$^{13}$C correlation experiments. Almost all cross peaks visible in the spectra are assigned, but only resonances from 43 of the 78 amino-acid residues could be detected. The missing residues are thought to be highly disordered and/or highly dynamic giving rise to broad resonance lines that escaped detection in the experiments applied. The line widths of the observed resonances are narrow and comparable to line widths observed in micro-crystalline samples. The 43 assigned residues are located in two fragments of about 20 residues.
Starting Page	75
Ending Page	87
Page Count	13
File Format	PDF
ISSN	09252738
Journal	Journal of Biomolecular NMR
Volume Number	34
Issue Number	2
e-ISSN	15735001
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2006-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	amyloid HET-s prions solid-state NMR Biochemistry Biophysics/Biomedical Physics Polymer Sciences
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Biochemistry

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