Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: Insights from molecular dynamics simulations

Protein aggregation into insoluble fibrillar structures known as amyloid characterizes several neurodegenerative diseases, including Alzheimer's, Huntington's and Creutzfeldt‐Jakob. Transthyretin (TTR), a homotetrameric plasma protein, is known to be the causative agent of amyloid patholog...

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Veröffentlicht in:	Protein science 2010-02, Vol.19 (2), p.202-219
Hauptverfasser:	Rodrigues, J. Rui, Simões, Carlos J. V., Silva, Cândida G., Brito, Rui M. M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer's disease amyloid Amyloid - chemistry Amyloid - metabolism amyloidogenic intermediates Crystallography, X-Ray Humans Hydrogen Bonding L55P‐TTR Models, Molecular molecular dynamics Molecular Dynamics Simulation Mutation Nuclear Magnetic Resonance, Biomolecular Prealbumin - chemistry Prealbumin - genetics Prealbumin - metabolism Protein Binding Protein Folding protein misfolding Protein Structure, Secondary Protein Structure, Tertiary protein unfolding transthyretin
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