Ann Marie Woys


Simple Method for Monitoring Protein Secondary Structure during Thermal Unfolding and Aggregation

March 16, 2016

Protein secondary structure during thermal unfolding and aggregation is readily acquired using IR spectroscopy and a temperature-controlled Mid-IR transmission accessory.

Simple Method for Monitoring Protein Secondary Structure During Thermal Unfolding and Aggregation

February 01, 2016

As the temperature increases, significant changes in the myoglobin secondary structure are observed. Between 25 °C and 70 °C, the 1649 cm-1 peak height decreases and linewidth increases. These changes in the amide I band reflect increased protein structural disorder. A temperature increase from 70 °C to 75 °C causes a drop in the 1649 cm-1 band intensity. Simultaneously, two peaks grow in at 1683 and 1637 cm-1. These changes indicate conversion of random coil/α-helix to intermolecular β-sheet. Further conversion to β-sheet is observed as the temperature rises to 90 °C. The final β-sheet structure is an insoluble aggregate. This aggregation process is not reversed when the temperature is driven back to 25 °C.