https://scholars.lib.ntu.edu.tw/handle/123456789/66918
標題: | Investigation of the Mechanism of β-Amyloid Fibril Formation by Kinetic and Thermodynamic Analyses | 作者: | Lin, Ming-Shen Chen, Liang-Yu Tsai, Hui-Ting Wang, Steven S.-S. Chang, Yung Higuchi, Akon Wang S.S.-S. |
公開日期: | 2008 | 卷: | 24 | 期: | 11 | 起(迄)頁: | 5802-5808 | 來源出版物: | Langmuir | URI: | http://ntur.lib.ntu.edu.tw//handle/246246/92281 | DOI: | 10.1021/la703369b | SDG/關鍵字: | 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 |
顯示於: | 化學工程學系 |
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