Back to search

Article

Extent of N-terminus exposure by altered long-range interactions of monomeric alpha-synuclein determines its aggregation propensity

2019-08-20

Abstract excerpt

As an intrinsically disordered protein, monomeric alpha synuclein (aSyn) constantly reconfigures and probes the conformational space. Long-range interactions across the protein maintain its solubility and mediate this dynamic flexibility, but also provide residual structure. Certain conformations lead to aggregation prone and non-aggregation prone intermediates, but identifying these within the dynamic ensemble of...

Topics

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

Identifiers and source

Literature Corpus work
a58a47e5-573c-5a27-a6bd-8eb0ff1bf898
DOI
10.1101/740241
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Extent of N-terminus exposure by altered long-range interactions of monomeric alpha-synuclein determines its aggregation propensityDOI 10.1101/740241
Select a neighboring publication to make it the new centre.