- Conference date: 29 Aug - 1 Sep 1999
- Location: Kobe-Sanda (Japan)
The aggregation of cytochrome c has been studied by 1D and 2D-IR spectroscopy in the presence of dimyristoylphosphatidylglycerol (DMPG). The influence of temperature on the aggregation has been evaluated by monitoring the intensity of a band at 1616 cm−1, which is characteristic of aggregated proteins. The results indicate that the extent of aggregation is increased with increasing temperatures and the 2D-IR correlation analysis has been used to correlate the various secondary structure components of cytochrome c during its aggregation. The results indicate that the first intermolecular bonds are formed between nearly native proteins. Then, the unfolding of α-helices allows further aggregation. Finally, the cytochrome c-DMPG complex was studied as a function of increasing temperature below its denaturation point in order to determine the nature of the amide bonds available for the formation of the first intermolecular bonds.
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