The fibrils of Ure2p homologs from Saccharomyces cerevisiae and Saccharoymyces paradoxus have similar cross-ß structure in both dried and hydrated forms.

Wang, Yi-Qian; Bongiovanni, Marie; Gras, Sally L; Perrett, Sarah

Wang, Yi-Qian; Bongiovanni, Marie; Gras, Sally L; Perrett, Sarah.

Affiliation

Wang YQ; National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.

J Struct Biol ; 174(3): 505-11, 2011 Jun.

Article in En | MEDLINE | ID: mdl-21419850

Subject(s)

Amyloid/ultrastructure; Glutathione Peroxidase/chemistry; Prions/chemistry; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae/chemistry; Amino Acid Sequence; Freeze Drying; Molecular Sequence Data; Scattering, Radiation; Sequence Alignment; Spectroscopy, Fourier Transform Infrared; X-Ray Diffraction

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Full text: 1 Database: MEDLINE Main subject: Saccharomyces cerevisiae / Prions / Protein Structure, Secondary / Saccharomyces cerevisiae Proteins / Glutathione Peroxidase / Amyloid Language: En Journal: J Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 2011 Type: Article Affiliation country: China

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