Techniques to elucidate the conformation of prions  

作　　者：Martin L Daus 

机构地区：[1]ZBS6-Proteomics and Spectroscopy, Robert Koch-Institute

出　　处：《World Journal of Biological Chemistry》2015年第3期218-222,共5页世界生物化学杂志（英文版）（电子版）

基　　金：Supported by Alberta Prion Research Institute,Canada(Project title:"Comprehensive Risk Assessment of CWD Transmission to Humans Using Non-human Primates");European Metrology Research Programme(EMRP);Researcher Grant:HLT10-Bi Origin(Metrology for the Biomolecular Origin of Disease)

摘　　要：Proteinaceous infectious particles(prions) are unique pathogens as they are devoid of any coding nucleic acid.Whilst it is assumed that prion disease is transmitted by a misfolded isoform of the cellular prion protein, the structural insight of prions is still vague and research for high resolution structural information of prions is still ongoing. In this review, techniques that may contribute to the clarification of the conformation of prions are presented and discussed.Proteinaceous infectious particles(prions) are unique pathogens as they are devoid of any coding nucleic acid.Whilst it is assumed that prion disease is transmitted by a misfolded isoform of the cellular prion protein, the structural insight of prions is still vague and research for high resolution structural information of prions is still ongoing. In this review, techniques that may contribute to the clarification of the conformation of prions are presented and discussed.

关 键 词：PRION AMYLOID NEURODEGENERATIVE disease Protein structure FOURIER-TRANSFORM infrared spectroscopy 

分 类 号：R373[医药卫生—病原生物学]