NDLI: Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p

Content Provider	Springer Nature Link
Author	Schütz, Anne K. Habenstein, Birgit Luckgei, Nina Bousset, Luc Sourigues, Yannick Nielsen, Anders B. Melki, Ronald Böckmann, Anja Meier, Beat H.
Copyright Year	2013
Abstract	Sup35p is a yeast prion and is responsible for the [PSI $^{+}$] trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated by X-ray crystallography or NMR in solution. We present solid-state NMR studies of fibrils formed by the full-length Sup35 protein. We detect an ordered and rigid core of the protein that gives rise to narrow and strong peaks, while large parts of the protein show either static disorder or dynamics on time scales which interfere with dipolar polarization transfer or shorten the coherence lifetime. Thus, only a small subset of resonances is observed in 3D spectra. Here we describe in detail the sequential assignments of the 22 residues for which resonances are observed in 3D spectra: their chemical shifts mostly corresponding to β-sheet secondary structure. We suspect that these residues form the amyloid core of the fibril.
Starting Page	349
Ending Page	356
Page Count	8
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	8
Issue Number	2
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2013-08-14
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Sup35p Fibrils Solid-state NMR Assignments structure Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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