The conformation of the prion domain of Sup35p in isolation and in the full-length protein

Autor: Carole Gardiennet, Birgit Habenstein, Yannick Sourigues, Anja Böckmann, Luc Bousset, Nina Luckgei, Anne K. Schütz, Ronald Melki, Beat H. Meier
Přispěvatelé: Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Physical Chemistry [ETH Zürich], Department of Chemistry and Applied Biosciences [ETH Zürich] (D-CHAB), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)- Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2013
Předmět:
Saccharomyces cerevisiae Proteins
Isolation (health care)
Prions
Protein Conformation
animal diseases
[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
Saccharomyces cerevisiae
macromolecular substances
010402 general chemistry
Fibril
01 natural sciences
Catalysis
Domain (software engineering)
03 medical and health sciences
MESH: Protein Structure
Tertiary
MESH: Prions
MESH: Protein Conformation
MESH: Saccharomyces cerevisiae Proteins
MESH: Nuclear Magnetic Resonance
Biomolecular
Nuclear Magnetic Resonance
Biomolecular
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
0303 health sciences
[SDV.NEU.PC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior
Chemistry
[SDV.NEU.SC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Cognitive Sciences
General Chemistry
MESH: Saccharomyces cerevisiae
Protein Structure
Tertiary
0104 chemical sciences
nervous system diseases
Biophysics
MESH: Peptide Termination Factors
Peptide Termination Factors
Zdroj: Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2013, 52 (48), pp.12741-4. ⟨10.1002/anie.201304699⟩
Angewandte Chemie-International Edition
Angewandte Chemie (International ed. in English)
ISSN: 1433-7851
1521-3773
DOI: 10.1002/anie.201304699⟩
Popis: The whole is not the sum of the parts: Fibrils form both from the full length Sup35 prion protein and also from its isolated NM domain. A conformation analysis of both shows that Sup35NM and fragments thereof which are often used as convenient models for prion fibril assembly have a very different conformation of the prion domains. Copyright © 2013 WILEY VCH Verlag GmbH Co. KGaA Weinheim.
Databáze: OpenAIRE
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