Structural Analysis of the Amyloid Fibrils Formed ofSyrian Hamster Prion Peptide (108-144) by UsingElectron Spin Resonance Spectroscopy
碩士 === 國立臺灣大學 === 生化科技學系 === 107 === Prion protein is a glycoprotein anchored on the membrane of neuron cells. The normal, cellular form (PrPC) is rich in α-helices. When PrPC is transformed to disease-causing form (PrPSc), β structures appear to dominate in prion protein. PrPSc is prone to associat...
Main Authors: | Yu-Sheng Lin, 林煜晟 |
---|---|
Other Authors: | Chien-Chih Yang |
Format: | Others |
Language: | en_US |
Published: |
2018
|
Online Access: | http://ndltd.ncl.edu.tw/handle/2hy9s5 |
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) -
Exploring the Amyloid Core Region of Hamster Prion Fibrils
by: Chih-Hao Shen, et al.
Published: (2015) -
Comparison of Molecular Structures of Protofibrils and Mature Fibrils Formed by Residues 113-127 of Syrian Hamster Prion Protein
by: Hsin-Mei Cheng, et al.
Published: (2009) -
Studies of the amyloid fibril formation of the prion peptides
by: Yen-Li Lee, et al.
Published: (2005) -
The Study of Amyloid Fibril Formation of Full-length Mouse Prion Protein and Short Mouse Prion Peptide
by: Chung-Yu Lee, et al.
Published: (2009)