Pregled bibliografske jedinice broj: 894880
Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy
Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy // Prions: Methods and Protocols / Lawson, Victoria A. (ur.).
Totowa (NJ): Humana Press, 2017. str. 35-49
CROSBI ID: 894880 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Analysis of Prion Protein Structure Using Nuclear
Magnetic Resonance Spectroscopy
Autori
Biljan, Ivana ; Ilc, Gregor ; Plavec, Janez
Vrsta, podvrsta i kategorija rada
Poglavlja u knjigama, znanstveni
Knjiga
Prions: Methods and Protocols
Urednik/ci
Lawson, Victoria A.
Izdavač
Humana Press
Grad
Totowa (NJ)
Godina
2017
Raspon stranica
35-49
ISBN
1493972421
Ključne riječi
Protein structure ; NMR structure determination ; Prion protein ; Mutants ; Prion diseases
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
