Nature Communications | Vol.8, Issue.1 | | Pages
Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
Aggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding energy landscape.
Original Text (This is the original text for your reference.)
Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
Aggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding energy landscape.
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Nicholas P. Reynolds,Jozef Adamcik,Joshua T. Berryman,Stephan Handschin,Ali Asghar Hakami Zanjani,Wen Li,Kun Liu,Afang Zhang,Raffaele Mezzenga,.Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides. 8 (1),.
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