Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Sup35pNM represents the N-terminal and middle (M) domains of the yeast Saccharomyces cerevisiae prion Sup35p. This fragment is commonly used for structural and functional studies of Sup35p. We here present a solid-state NMR study of fibrils formed by this fragment and show that sequential assignments can be obtained for the rigid and well-ordered parts of the protein using 3D spectroscopy. We describe in detail the sequential assignment of the 22 residues yielding strong, narrow signals with chemical shifts that correspond mostly to β-sheet secondary-structured amino acids that form the fibril core.
Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon, 1, 7 passage du Vercors, 69367, Lyon, France.
Nina
N
Luckgei
Anne K
AK
Schütz
Birgit
B
Habenstein
Luc
L
Bousset
Yannick
Y
Sourigues
Ronald
R
Melki
Beat H
BH
Meier
Anja
A
Böckmann
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010454:Peptide Termination Factors / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
D000682:Amyloid; D010454:Peptide Termination Factors; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins