Directed destabilization of lysozyme in protic ionic liquids reveals a compact, low energy, soluble, reversibly-unfolding (pre-fibril) state

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dc.creatorByrne, Nolene
dc.creatorBelieres, Jean-Philippe
dc.creatorAngell, C. Austen
dc.date2007-10-20
dc.date.accessioned2026-07-07T08:37:33Z
dc.date.available2026-07-07T08:37:33Z
dc.descriptionRecent demonstrations of extraordinary stabilization of proteins in mobile protic [1] and aprotic [2] ionic liquid solutions at ambient temperatures have raised hopes of new biopreservation and drug transportation technologies. Here we examine the relation of folded protein stability to the state of the transferred proton [1], as determined by the N-H proton chemical shift, d(N-H). We identify a range of d(N-H) in which the unfolded lysozyme refolds 97%. Exceeding the stability range in the acid direction leads to the sudden formation and stabilization of a small, soluble, amyloid form of lysozyme which has its own stability range and which can again unfold/refold many times before an irreversible process, fibrillization, occurs. The tightly bound amyloid form of the lysozyme molecule, identified by circular dichroism spectra and dynamic light scattering, must be of very low energy since the unfolding process absorbs almost three times the enthalpy of normal lysozyme unfolding. alpha-lactalbumin shows similar behavior.
dc.description12 pages, 4 figures
dc.identifierhttps://arxiv.org/abs/0710.3807
dc.identifierhttp://arxiv.org/abs/0710.3807
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/140439
dc.subjectBiological Physics
dc.subjectChemical Physics
dc.titleDirected destabilization of lysozyme in protic ionic liquids reveals a compact, low energy, soluble, reversibly-unfolding (pre-fibril) state
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