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Article

Position-dependent electrostatic protection against protein aggregation.

Chembiochem : a European journal of chemical biology - 25 May 2009

Buell Alexander K, Tartaglia Gian Gaetano, Birkett Neil R, Waudby Christopher A, Vendruscolo Michele, Salvatella Xavier, Welland Mark E, Dobson Christopher M, Knowles Tuomas P J

Abstract excerpt

Proteins with a high propensity to aggregate can be largely prevented from doing so with surprisingly small changes to their primary structure. By using a combination of rational design and quantitative measurements of aggregation rates, we show that adding a single charge in specific "gatekeeper" regions is sufficient to change the timescale for amyloid fibril growth from minutes to weeks, thereby dramatically...

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Identifiers

PMID: 19415709
DOI: 10.1002/cbic.200900144

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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