Phase Diagram of alpha-Helical and beta-Sheet Forming Peptides

Abstract

The intrinsic property of proteins to form structural motifs such as alpha-helices and beta-sheets leads to a complex phase behavior in which proteins can assemble into various types of aggregates including crystals, liquidlike phases of unfolded or natively folded proteins, and amyloid fibrils. Here we use a coarse-grained protein model that enables us to perform Monte Carlo simulations for determining the phase diagram of natively folded alpha-helical and unfolded beta-sheet forming peptides. The simulations reveal the existence of various metastable peptide phases. The liquidlike phases are metastable with respect to the fibrillar phases, and there is a hierarchy of metastability.

References in corpus (1)

• Self-Templated Nucleation in Peptide and Protein aggregation

Cited by in corpus (5)

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• Aggregate geometry in amyloid fibril nucleation
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• Universality in the morphology and mechanics of coarsening amyloid fibril networks
• Protein sequence and structure: Is one more fundamental than the other?