We have used the fluorescence anisotropy (FA) decay of retinol bound to bovine b-lactoglobulin to monitor the time evolution of protein aggregation during the early stages of crystal growth. With this approach we have followed the formationof aggregates at different concentrations of ammonium sulfate, the precipitant used for crystallization. The average aggregation number is found to depend on precipitant concentration, and to be restricted to small numbers ranging from 2 to 5, also in the presence of visible growing crystals. The effect of particle distributionan d of low probe-to-proteinsaturationonthe FA response is also discussed in detail.
Probing protein aggregation by time resolved fluorescence during beta-lactoglobulin crystal growth
MONACO, Ugo Luigi;
2001-01-01
Abstract
We have used the fluorescence anisotropy (FA) decay of retinol bound to bovine b-lactoglobulin to monitor the time evolution of protein aggregation during the early stages of crystal growth. With this approach we have followed the formationof aggregates at different concentrations of ammonium sulfate, the precipitant used for crystallization. The average aggregation number is found to depend on precipitant concentration, and to be restricted to small numbers ranging from 2 to 5, also in the presence of visible growing crystals. The effect of particle distributionan d of low probe-to-proteinsaturationonthe FA response is also discussed in detail.
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