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Zhang L, Schmit JD. Theory of amyloid fibril nucleation from folded proteins. Isr J Chem. 2017;57(7):738-749doi: 10.1002/ijch.201600079.
Zhang, L., & Schmit, J. D. (2017). Theory of amyloid fibril nucleation from folded proteins. Israel journal of chemistry, 57(7), 738-749. https://doi.org/10.1002/ijch.201600079
Zhang, Lingyun, and Schmit, Jeremy D. "Theory of amyloid fibril nucleation from folded proteins." Israel journal of chemistry vol. 57,7 (2017): 738-749. doi: https://doi.org/10.1002/ijch.201600079
Zhang L, Schmit JD. Theory of amyloid fibril nucleation from folded proteins. Isr J Chem. 2017 Jul;57(7):738-749. doi: 10.1002/ijch.201600079. Epub 2017 Jan 30. PMID: 28935998; PMCID: PMC5602581.
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Isr J Chem. 2017 Jul;57(7):738-749. doi: 10.1002/ijch.201600079. Epub 2017 Jan 30.

Theory of amyloid fibril nucleation from folded proteins.

Israel journal of chemistry

Lingyun Zhang, Jeremy D Schmit

Affiliations

  1. Department of Physics, Kansas State University, Manhattan, KS 66506, USA.
  2. Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.

PMID: 28935998 PMCID: PMC5602581 DOI: 10.1002/ijch.201600079

Abstract

We present a theoretical model for the nucleation of amyloid fibrils. In our model we use helix-coil theory to describe the equilibrium between a soluble native state and an aggregation-prone unfolded state. We then extend the theory to include oligomers with

Keywords: Amyloid beta-peptides; Biophysics; Fibrous proteins; Protein models; aggregation

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