Physics – Biological Physics
Scientific paper
2007-10-20
Physics
Biological Physics
12 pages, 4 figures
Scientific paper
Recent 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.
Angell Austen C.
Belieres Jean-Philippe
Byrne Nolene
No associations
LandOfFree
Directed destabilization of lysozyme in protic ionic liquids reveals a compact, low energy, soluble, reversibly-unfolding (pre-fibril) state does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Directed destabilization of lysozyme in protic ionic liquids reveals a compact, low energy, soluble, reversibly-unfolding (pre-fibril) state, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Directed destabilization of lysozyme in protic ionic liquids reveals a compact, low energy, soluble, reversibly-unfolding (pre-fibril) state will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-477202