The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
Cordeiro, Yraima
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. [electronic resource] - Biophysical journal Oct 2005 - 2667-76 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-3495
10.1529/biophysj.105.067603 doi
Amino Acid Substitution
Animals
Binding Sites
Dimerization
Mice
Multiprotein Complexes--analysis
Mutagenesis, Site-Directed
Prions--analysis
Protein Binding
Protein Conformation
Protein Denaturation
Protein Folding
Protein Structure, Tertiary
Recombinant Proteins--analysis
Structure-Activity Relationship
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. [electronic resource] - Biophysical journal Oct 2005 - 2667-76 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-3495
10.1529/biophysj.105.067603 doi
Amino Acid Substitution
Animals
Binding Sites
Dimerization
Mice
Multiprotein Complexes--analysis
Mutagenesis, Site-Directed
Prions--analysis
Protein Binding
Protein Conformation
Protein Denaturation
Protein Folding
Protein Structure, Tertiary
Recombinant Proteins--analysis
Structure-Activity Relationship