Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
Ishimaru, Daniella
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain. [electronic resource] - Biophysical journal Oct 2004 - 2691-700 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-3495
10.1529/biophysj.104.044685 doi
Dimerization
Guanidine--chemistry
Kinetics
Multiprotein Complexes--chemistry
Protein Conformation
Protein Folding
Protein Structure, Tertiary
Tumor Suppressor Protein p53--chemistry
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain. [electronic resource] - Biophysical journal Oct 2004 - 2691-700 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-3495
10.1529/biophysj.104.044685 doi
Dimerization
Guanidine--chemistry
Kinetics
Multiprotein Complexes--chemistry
Protein Conformation
Protein Folding
Protein Structure, Tertiary
Tumor Suppressor Protein p53--chemistry