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000904306 1001_ $$0P:(DE-Juel1)151182$$aBarz, Bogdan$$b0$$eCorresponding author
000904306 245__ $$aCompact fibril-like structure of amyloid β-peptide (1–42) monomers
000904306 260__ $$aCambridge$$bSoc.$$c2021
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000904306 520__ $$aAmyloid β (Aβ) monomers are the smallest assembly units, and play an important role in most of the individual processes involved in amyloid fibril formation. An important question is whether the monomer can adopt transient fibril-like conformations in solution. Here we use enhanced sampling simulations to study the Aβ42 monomer structural flexibility. We show that the monomer frequently adopts conformations with the N-terminus region structured very similarly to the conformation it adopts inside the fibril. This intrinsic propensity of monomeric Aβ to adopt fibril-like conformations could explain the low free energy barrier for Aβ42 fibril elongation.
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000904306 7001_ $$00000-0003-1161-3622$$aBuell, Alexander K.$$b1
000904306 7001_ $$00000-0003-2330-3621$$aNath, Soumav$$b2
000904306 773__ $$0PERI:(DE-600)1472881-3$$a10.1039/D0CC06607A$$gVol. 57, no. 7, p. 947 - 950$$n7$$p947 - 950$$tChemical communications$$v57$$x0009-241X$$y2021
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