Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9757452 | Vibrational Spectroscopy | 2005 | 6 Pages |
Abstract
We have investigated the temperature induced denaturation and aggregation of the recombinant fragment SHaPrP90-232 of the hamster prion protein by Fourier transform infrared (FTIR) spectroscopy in H2O and D2O buffers. Difference spectra of this denaturation/aggregation reaction revealed a decrease of α-helical and turn structures and an increase of intermolecularly formed antiparallel β-sheet structure. Compared to previously examined critical oligomers in H2O buffer, the temperature induced aggregates of SHaPrP90-232 exhibited a less rigid but still strong hydrogen bonding pattern as indicated by the β-sheet specific difference band at 1624 cmâ1. The denaturation/aggregation temperature of SHaPrP90-232 was consistently determined using the β-sheet specific difference band observed in the H2O or in the D2O experiments. Further, the spectra obtained for the critical oligomers produced in appropriate buffer systems at 25 °C and at 37 °C revealed no significant differences in secondary structure.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Fabian Sokolowski, Dieter Naumann,