Lin, Ming-ShenMing-ShenLinChen, Liang-YuLiang-YuChenTsai, Hui-TingHui-TingTsaiWang, Steven S.-S.Steven S.-S.WangChang, YungYungChangHiguchi, AkonAkonHiguchiWang S.S.-S.2008-12-172018-06-282008-12-172018-06-282008http://ntur.lib.ntu.edu.tw//handle/246246/92281application/pdf810030 bytesapplication/pdfen-US[SDGs]SDG3Agglomeration; 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, Secondaryjournal article10.1021/la703369b2-s2.0-45749097124http://ntur.lib.ntu.edu.tw/bitstream/246246/92281/1/23.pdf