Article

Exceptional aggregation propensity of amino acids in polyglutamine amino-acid-homopolymer

2020-07-10

Abstract excerpt

Similar aggregation and β-sheet propensity of amino acids in globular proteins and amyloids, suggests comparable principles of their formation. Here we show that during the process of aggregation into amyloid-like fibers, these rules are not the same in an amino-acid-homopolymer (AAHP) polyglutamine (PolyGln). An aggregation kinetic analysis on nine-point mutants of a forty-six long PolyGln peptide was carried in...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: c9a3408f-fa81-51bf-bbf6-94b5961e6eab
DOI: 10.1101/2020.07.09.194753

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Exceptional aggregation propensity of amino acids in polyglutamine amino-acid-homopolymerDOI 10.1101/2020.07.09.194753Read

Structure propensities in mutated polyglutamine peptides.Semantic proximity Read

Polyglutamine aggregation in Huntington and related diseases.Semantic proximity Read

The structural plasticity of polyglutamine repeatsSemantic proximity Read

Monomeric, Oligomeric and Polymeric Proteins in Huntington Disease and Other Diseases of Polyglutamine ExpansionSemantic proximity Read

Mutation effects on structural stability of polyglutamine peptides by molecular dynamics simulation.Semantic proximity Read

Neurotoxic protein oligomerisation associated with polyglutamine diseases.Semantic proximity Read

To What Extent is Anfinsen’s Thermodynamic Hypothesis Consistent With the Formation and Polymorphism of Amyloid Fibrils?Semantic proximity Read

The β-turn-supporting motif in the polyglutamine binding peptide QBP1 is essential for inhibiting huntingtin aggregation.Semantic proximity Read

Probing the energy landscape of α-Synuclein amyloid fibril formation by systematic K-to-Q mutagenesisSemantic proximity Read

Unraveling the aggregation dynamics of amyloidogenesis: A data-driven mathematical modeling approachSemantic proximity Read

Structural analysis of oligomeric and protofibrillar Aβ amyloid pair structures considering F20L mutation effects using molecular dynamics simulations.Semantic proximity Read

Amyloid nanospheres from polyglutamine rich peptides: assemblage through an intermolecular salt bridge interaction.Semantic proximity Read