Article

pH Induced Switch in the Conformational Ensemble of an Intrinsically Disordered Protein Prothymosin- <i>α</i> and Its Implications to Amyloid Fibril Formation

2022-06-29

Abstract excerpt

Aggregation of intrinsically disordered proteins (IDPs) is the cause of various neu-rodegenerative diseases. Changes in solution pH can trigger IDP aggregation due to a shift in the IDP monomer population with a high aggregation propensity. Al-though there is experimental evidence that acidic pH promotes the compaction of IDP monomers, which subsequently leads to aggregation, the general mechanism is not clear. Us...

Topics

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

Identifiers and source

Literature Corpus work: 27521729-2bab-5183-9f74-f5b4ccb0cc61
DOI: 10.1101/2022.06.25.497626

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

pH Induced Switch in the Conformational Ensemble of an Intrinsically Disordered Protein Prothymosin- <i>α</i> and Its Implications to Amyloid Fibril FormationDOI 10.1101/2022.06.25.497626Read

Histidine tautomerism dependent conformational transitions driven aggregation of profilin-1: Implications in amyotrophic lateral sclerosis.Semantic proximity Read

Surface electrostatic networks control hydrophobic core remodeling in a pH-dependent switching proteinSemantic proximity Read

The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality controlSemantic proximity Read

Zinc Determines Dynamical Properties and Aggregation Kinetics of Human InsulinSemantic proximity Read

Combined Effects of Mutation and Ionic Strength on α-Synuclein Reveal Generic Features of Aggregation-Prone Monomeric States.Semantic proximity Read

Molecular and Functional Profiling of Gαi as an Intracellular pH SensorSemantic proximity Read

pH driven fibrillar aggregation of the super-sweet protein Y65R-MNEI: A step-by-step structural analysis.Semantic proximity Read

A Self-Consistent Molecular Mechanism of β2-Microglobulin Aggregation.Semantic proximity Read

Exceptional aggregation propensity of amino acids in polyglutamine amino-acid-homopolymerSemantic proximity Read

Sequence-encoded conformational biases shape self-assembly modes of intrinsically disordered proteinsSemantic proximity Read

Exploring the pH-dependent structure-dynamics-function relationship of human reninSemantic proximity Read

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesSemantic proximity Read