Exploring the Amyloid Core Region of Hamster Prion Fibrils
碩士 === 國立臺灣大學 === 生化科學研究所 === 103 === The prion diseases are transmissible fatal neurodegenerative disorders affecting human and other mammals. One of the crucial molecular events is the conformational conversion of the normal, membrane-anchored prion protein PrP(C) into the β-sheet-rich and misfold...
Main Authors: | Chih-Hao Shen, 沈志豪 |
---|---|
Other Authors: | 陳佩燁 |
Format: | Others |
Language: | en_US |
Published: |
2015
|
Online Access: | http://ndltd.ncl.edu.tw/handle/78044877869733959324 |
Similar Items
-
Solid-state NMR Study of Amyloid Fibrils Formed by Residues 109—122 of the Syrian Hamster Prion Protein
by: Hsin-Wen Lee, et al.
Published: (2007) -
Studies of the amyloid fibril formation of the prion peptides
by: Yen-Li Lee, et al.
Published: (2005) -
Structural Analysis of the Amyloid Fibrils Formed ofSyrian Hamster Prion Peptide (108-144) by UsingElectron Spin Resonance Spectroscopy
by: Yu-Sheng Lin, et al.
Published: (2018) -
Molecular Dynamics and Density Functional Theory Investigation on the Structures and Characteristics of Prion Protein Amyloid Fibrils
by: John Ching-Hao Chao, et al.
Published: (2010) -
Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils
by: Mantas Ziaunys, et al.
Published: (2021-05-01)