Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy (CROSBI ID 59427)
Prilog u knjizi | izvorni znanstveni rad
Podaci o odgovornosti
Biljan, Ivana ; Ilc, Gregor ; Plavec, Janez
engleski
Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy
Nuclear magnetic resonance (NMR) spectroscopy is a powerful experimental tool for obtaining information on three-dimensional (3D) structures of proteins at atomic resolution. In inherited forms of prion diseases, misfolding of cellular prion protein, PrPC, into its pathological form, PrPSc, is caused by mutations in the human prion protein gene (PRNP). Understanding of the earliest stages of the conformational changes leading to spontaneous generation of prions in inherited forms of prion diseases may benefit from detailed structural analysis of different human (Hu) PrP variants. Here, we describe the protocol for structure determination of HuPrP variants by NMR spectroscopy in solution that consists of preparation of NMR samples, acquisition of NMR data, NMR resonance assignments, and structure calculation.
Protein structure ; NMR structure determination ; Prion protein ; Mutants ; Prion diseases
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
Podaci o prilogu
35-49.
objavljeno
Podaci o knjizi
Prions: Methods and Protocols
Lawson, Victoria A.
Totowa (NJ): Humana Press
2017.
1493972421