Abstract
During protein folding or unfolding, population of intermediates or partially unfolded conformations that tend to aggregate, can occur. A possible result of this aggregation are fibrils, which are the hallmark of molecular diseases such as Alzheimer’s disease. It has been suggested that in vitro fibril formation is a generic property of all proteins. In this work, insulin has been chosen as a model protein to follow the process of fibril formation with Fourier transform infrared (FTIR) spectroscopy. The activation energy is calculated for the wild type (WT) insulin as well as for one of its mutants, des-pentapeptide insulin (DPI). The activation volume could not be calculated since low pressures (20 MPa) are sufficient to inhibit insulin fibrillogenesis. This suggests that the activation volume is very high.
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Dirix, C., Esters, I., Meersman, F., Heremans, K. (2003). Temperature/Pressure Study of Insulin Fibrillogenesis. In: Winter, R. (eds) Advances in High Pressure Bioscience and Biotechnology II. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-05613-4_26
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DOI: https://doi.org/10.1007/978-3-662-05613-4_26
Publisher Name: Springer, Berlin, Heidelberg
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