Colloidal-like aggregation of a functional amyloid protein
Author:
Affiliation:
1. Institute of Chemistry
2. The Hebrew University of Jerusalem and The Center for Nanoscience and Nanotechnology
3. Edmond J. Safra Campus
4. Jerusalem 91904
5. Israel
6. The Israel Institute for Biological Research
7. Ness Ziona
Abstract
TasA, a bacterial functional amyloid protein, aggregates in a colloidal – like mechanism upon exposure to acidic conditions.
Funder
Israel Science Foundation
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2020/CP/D0CP03265D
Reference39 articles.
1. Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications
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3. Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation
4. Partially Unfolded States of β2-Microglobulin and Amyloid Formation in Vitro
5. Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17
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