Understanding the Effect of Disease-Related Mutations on Human Prion Protein Structure: Insights From NMR Spectroscopy (CROSBI ID 60038)
Prilog u knjizi | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Biljan, Ivana ; Ilc, Gregor ; Plavec, Janez
engleski
Understanding the Effect of Disease-Related Mutations on Human Prion Protein Structure: Insights From NMR Spectroscopy
Prion diseases or transmissible spongiform encephalopathies constitute a group of fatal neurodegenerative diseases that can be of sporadic, genetic, or acquired origin. The central molecular event of prion diseases is the conformational conversion of the physiological cellular prion protein, PrPC, into a disease-associated form known as prion or PrPSc. Spontaneous generation of prions in genetic prion diseases is caused by mutations in the human prion protein gene (PRNP). Understanding of the earliest conformational changes during misfolding of PrPC in genetic forms of prion diseases may benefit from detailed structural characterization of various human (Hu) PrP variants. Nuclear magnetic resonance (NMR) spectroscopy offers unique opportunities to obtain detailed atomic-level structure information. In this chapter we present an overview of high-resolution NMR studies on several HuPrPs with disease- associated mutations at mildly acidic and physiological pH conditions that provided valuable insights into possible key structural determinants underlying the formation of prions.
Prion protein ; Prion diseases ; NMR spectroscopy ; Structure determination ; Mutants ; Protective polymorphism ; pH
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Podaci o prilogu
83-103.
objavljeno
10.1016/bs.pmbts.2017.06.006
Podaci o knjizi
Prion Protein
Legname, Giuseppe ; Vanni, Silvia
San Diego (CA): Elsevier
2017.
978-0-12-811227-4
1877-1173
Povezanost rada
Kemija