Kheterpal I, Chen M, Cook KD, Wetzel R.
Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange--mass spectrometry with on-line proteolytic fragmentation.
J Mol Biol. 2006 Aug 25;361(4):785-95.
PubMed.
This paper is interesting because it describes some of the structural differences between Aβ fibrils and oligomers, and there is very little known about oligomer structure. The data indicate that while some regions are similarly disordered in fibrils and oligomers, the internal region from residues 20-30 is less protected from hydrogen-deuterium exchange. This suggests that oligomers may transition to fibrils by a change in the ordering in this region.
Comments
University of California, Irvine
This paper is interesting because it describes some of the structural differences between Aβ fibrils and oligomers, and there is very little known about oligomer structure. The data indicate that while some regions are similarly disordered in fibrils and oligomers, the internal region from residues 20-30 is less protected from hydrogen-deuterium exchange. This suggests that oligomers may transition to fibrils by a change in the ordering in this region.
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