Abstract
Aggregation of globular proteins into fibrils seems to be a generic form of aggregation.
However, the exact mechanism of fibril formation is still unclear. One of the questions
is whether the aggregation is an enthalpy- or an entropy-driven process. We measured the
critical aggregation concentration versus temperature for the fibril formation of ß-lg at
pH 2 and used this data to calculate the thermodynamic parameters for the aggregation
process.
Keywords: fibrillar aggregation, CAC, binding energy, entropy
Original language | English |
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Publication status | Published - 2007 |
Event | Nationale MicroNano Conferentie - Duration: 15 Nov 2007 → 16 Nov 2007 |
Conference/symposium
Conference/symposium | Nationale MicroNano Conferentie |
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Period | 15/11/07 → 16/11/07 |