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Analysis of Prion Protein Structure Using Nuclear Magnetic Resonance Spectroscopy (CROSBI ID 59427)

Prilog u knjizi | izvorni znanstveni rad

Biljan, Ivana ; Ilc, Gregor ; Plavec, Janez 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

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

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Podaci o prilogu

35-49.

objavljeno

Podaci o knjizi

Prions: Methods and Protocols

Lawson, Victoria A.

Totowa (NJ): Humana Press

2017.

1493972421

Povezanost rada

Kemija