Luckgei Nina, Schütz Anne K, Habenstein Birgit, Bousset Luc, Sourigues Yannick, Melki Ronald, Meier Beat H, Böckmann Anja
Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon, 1, 7 passage du Vercors, 69367, Lyon, France.
Biomol NMR Assign. 2014 Oct;8(2):365-70. doi: 10.1007/s12104-013-9518-y. Epub 2013 Aug 10.
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.
Sup35pNM代表酿酒酵母朊病毒Sup35p的N端和中间（M）结构域。该片段常用于Sup35p的结构和功能研究。我们在此展示了对该片段形成的纤维进行的固态核磁共振研究，并表明使用三维光谱可以获得该蛋白质刚性且有序部分的序列归属。我们详细描述了22个残基的序列归属，这些残基产生强而窄的信号，其化学位移大多对应于形成纤维核心的β折叠二级结构氨基酸。
