Simple Method for Monitoring Protein Secondary Structure During Thermal Unfolding and Aggregation
February 1st 2016As 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.
Infrared Transmission Measurements of Diffuse Samples
September 1st 2015Measuring the transmission of diffuse samples such as paper or filled polymer films requires an integrating sphere to obtain accurate transmission values and useful chemical information, because the IR light is scattered as it passes through the sample. An integrating sphere serves as a collection device for the scattered light.
Rapid Micro-Sampling by ATR/FT-IR
September 1st 2009In ATR/FT-IR, magnified visual monitoring of a sample benefits many applications. For micro-sampling and defect analysis, viewing capabilities decrease overall measurement time by allowing the user to locate the desired sampling area quickly and enhance confidence in the collected data by assuring the sampling point. Visual changes in the sample also may be easily monitored during testing. As an example application, the ease of micro-sampling is shown through fiber analysis and the results are discussed.