Two prion variants of Sup35p have in-register parallel β-sheet structures, independent of hydration

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5074-5082

  Shewmaker, Frank ^a   Kryndushkin, Dmitry ^a   Chen, Bo ^a   Tycko, Robert ^a   Wickner, Reed B ^a,b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID STRUCTURES; BIOLOGICAL PROPERTIES; C-DOMAIN; C-TERMINAL DOMAINS; ELONGATION FACTOR; HYDRATED FORMS; LEUCINE RESIDUES; SELF-PROPAGATING; SHEET STRUCTURE; SOLID STATE NMR;

AMINES; AMINO ACIDS; BEAM PLASMA INTERACTIONS; HYDRATES; HYDRATION;

GLYCOPROTEINS;

AMYLOID PROTEIN; LEUCINE; PRION PROTEIN; PROTEIN SUP35; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; CONTROLLED STUDY; FREEZE DRYING; HYDRATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTEIN VARIANT; SOLID STATE; YEAST;

AMINO ACID SEQUENCE; AMYLOID; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PRIONS; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; TEMPERATURE; TRANSFECTION;

EUKARYOTA;

EID: 67049087912     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900345q     Document Type: Article

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