Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: A quantitative analysis of the effects of pH and buffer system

Journal of Molecular Biology

Volumn 328, Issue 1, 2003, Pages 235-254

  Zhu, Li ^a   Zhang, Xu Jia ^a   Wang, Ling Yun ^a   Zhou, Jun Mei ^a   Perrett, Sarah ^a  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Dissociation; First order kinetics; Nucleation; Protein folding; Protein stability

Indexed keywords

AMYLOID; BUFFER; DIMER; MONOMER; PHOSPHATE; PRION PROTEIN; PROTEIN; THIOFLAVINE; TROMETAMOL;

ARTICLE; CONCENTRATION (PARAMETERS); DISSOCIATION; ENERGY; FIBER; FLUORESCENCE; KINETICS; MODEL; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; TEMPERATURE; THERMODYNAMICS; YEAST;

EID: 0037453298     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00249-3     Document Type: Article

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