The peculiar nature of unfolding of the human prion protein

Keyphrases

• Amyloid Fibrils 33%
• C-terminal Fragments 33%
• Circular Dichroism Spectroscopy 33%
• Conformational Transition 33%
• Denaturation 33%
• Denatured State 33%
• Denaturing Conditions 33%
• Efficiency Increase 33%
• Energy Transfer 33%
• Environmental Conditions 33%
• Fibril Formation 33%
• Folded State 33%
• Lag Phase 66%
• Middle Points 33%
• Native Species 33%
• Pathologic Conditions 33%
• Prion Disease 33%
• Prion Protein 100%
• PrPC 33%
• Rate-limiting Step 33%
• Recombinant Human 33%
• Size Exclusion Chromatography 33%
• Spontaneous Transformation 33%
• Sulfonate 33%
• Thermodynamic Parameters 33%
• Thermodynamics 33%
• Unfolding Intermediates 66%
• Urea 100%
• Urea Denaturation 33%
• Variable Model 33%

Biochemistry, Genetics and Molecular Biology

• Amyloid Protein 50%
• C-Terminus 50%
• Circular Dichroism 50%
• Conformation 50%
• Conformational Change 50%
• Denaturation 100%
• Denatured State 50%
• Energy Transfer 50%
• Isoform 100%
• Native Species 50%
• Prion Protein 100%
• Size-Exclusion Chromatography 50%
• Sulfonate 50%
• Transmissible Spongiform Encephalopathy 50%