Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.
Rodriguez, Roberto A
Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline. [electronic resource] - Biochemical and biophysical research communications 05 2017 - 444-449 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1090-2104
10.1016/j.bbrc.2017.04.084 doi
Amyloid--chemistry
Amyloid beta-Peptides--chemistry
Binding Sites
Biomimetic Materials--chemistry
Body Fluids--chemistry
Drug Stability
Models, Chemical
Molecular Docking Simulation
Peptide Fragments--chemistry
Protein Binding
Protein Conformation
Protein Multimerization
Sodium Chloride--chemistry
Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline. [electronic resource] - Biochemical and biophysical research communications 05 2017 - 444-449 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1090-2104
10.1016/j.bbrc.2017.04.084 doi
Amyloid--chemistry
Amyloid beta-Peptides--chemistry
Binding Sites
Biomimetic Materials--chemistry
Body Fluids--chemistry
Drug Stability
Models, Chemical
Molecular Docking Simulation
Peptide Fragments--chemistry
Protein Binding
Protein Conformation
Protein Multimerization
Sodium Chloride--chemistry