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2011 | OriginalPaper | Buchkapitel

Molecular Dynamics as an Approach to Study Prion Protein Misfolding and the Effect of Pathogenic Mutations

verfasst von : Marc W. van der Kamp, Valerie Daggett

Erschienen in: Prion Proteins

Verlag: Springer Berlin Heidelberg

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Abstract

Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes can be simulated, including the initial steps of misfolding. By introducing mutations in silico, the effect of pathogenic mutations on PrP conformation and dynamics can be assessed. Here, we briefly introduce molecular dynamics methods and review the application of molecular dynamics simulations to obtain insight into various aspects of the PrP, including the mechanism of misfolding, the response to changes in the environment, and the influence of disease-related mutations.

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Vorheriges Kapitel Prion Protein and Its Conformational Conversion: A Structural Perspective

Nächstes Kapitel Chemical Biology of Prion Protein: Tools to Bridge the In Vitro/Vivo Interface

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Titel: Molecular Dynamics as an Approach to Study Prion Protein Misfolding and the Effect of Pathogenic Mutations
verfasst von: Marc W. van der Kamp
Valerie Daggett
Verlag: Springer Berlin Heidelberg
Buch: Prion Proteins
Print ISBN: 978-3-642-24066-9

Electronic ISBN: 978-3-642-24067-6

Copyright-Jahr: 2011
DOI: https://doi.org/10.1007/128_2011_158