Investigation of the Mechanism of β-Amyloid Fibril Formation by Kinetic and Thermodynamic Analyses
Resource
Langmuir 24 (11): 5802-5808
Journal
Langmuir
Journal Volume
24
Journal Issue
11
Pages
5802-5808
Date Issued
2008
Date
2008
Author(s)
SDGs
Other Subjects
Agglomeration; Conformations; Deposits; Dichroism; Dynamics; Epitaxial growth; Forming; Glycoproteins; Hydrophobicity; Mechanics; Mechanisms; Microfluidics; Nucleation; Optical properties; pH; pH effects; Rate constants; Thermoanalysis; Thermodynamic properties; Thermodynamics; Volumetric analysis; (p ,p ,t) measurements; Aggregation processing; Alzheimer's disease (AD); American Chemical Society (ACS); amyloid fibril formation; Circular dichroism (DC); driving forces; Environmental factors; Extracellular; fluorescence assays; Hydrophobic (hydrophilic) force; Hydrophobic interactions; Isothermal titration calorimetry (ITC); Kinetic (Polym.); Kinetics and thermodynamics; Primary factors; Rate determining step (RDS); secondary structures; Sheet structures; Strength (IGC: D5/D6); Two state models; Ionic strength; amyloid; amyloid beta protein; amyloid beta protein[1-40]; peptide fragment; animal; article; chemistry; heat; human; hydrophobicity; kinetics; pH; protein quaternary structure; protein secondary structure; Amyloid; Amyloid beta-Protein; Animals; Heat; Humans; Hydrogen-Ion Concentration; Hydrophobicity; Kinetics; Peptide Fragments; Protein Structure, Quaternary; Protein Structure, Secondary
Type
journal article
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