Modulation of the aggregation of an amyloidogenic sequence by flanking-disordered region in the intrinsically disordered antigen merozoite surface protein 2
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
http://link.springer.com/article/10.1007/s00249-018-1337-8/fulltext.html
Reference48 articles.
1. Abedini A, Raleigh DP (2009) A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Phys Biol 6:015005. https://doi.org/10.1088/1478-3975/6/1/015005
2. Abeln S, Frenkel D (2008) Disordered flanks prevent peptide aggregation. PLoS Comput Biol 4:e1000241. https://doi.org/10.1371/journal.pcbi.1000241
3. Adda CG et al (2009) Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils. Mol Biochem Parasitol 166:159–171. https://doi.org/10.1016/j.molbiopara.2009.03.012
4. Ahmed AB, Kajava AV (2013) Breaking the amyloidogenicity code: methods to predict amyloids from amino acid sequence. FEBS Lett 587:1089–1095. https://doi.org/10.1016/j.febslet.2012.12.006
5. Bhattacherjee A, Wallin S (2012) Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks. Biophys J 102:569–578. https://doi.org/10.1016/j.bpj.2011.12.008
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