Shining Light On Protein's to 'See* their Characteristics

Presenter Information

Start Date

April 2026

Location

3rd floor - Library

Abstract

Spectroscopy is the study of how light interacts with material whether it be absorption or fluorescence. Specifically, the interaction of light with proteins can be used to study their structure and provide insights into their stability. We have access to an instrument that can use several spectroscopy techniques such as circular dichroism, absorption, and fluorescence to infer such protein characteristics. Circular dichroism (CD) spectroscopy, the difference in absorption between circular polarized light, is a helpful technique when studying the percentage of secondary structures such as α-helices and β-sheets of a protein. Fluorescence, the emission of light, can be monitored during experiments where the protein becomes unfolded. The signal change of fluorescence during an unfolding curve using a chemical denaturant is presented here to determine the free energy between the folded and unfolded state of the model protein Cytochrome c.

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Apr 22nd, 2:25 PM Apr 22nd, 3:25 PM

Shining Light On Protein's to 'See* their Characteristics

3rd floor - Library

Spectroscopy is the study of how light interacts with material whether it be absorption or fluorescence. Specifically, the interaction of light with proteins can be used to study their structure and provide insights into their stability. We have access to an instrument that can use several spectroscopy techniques such as circular dichroism, absorption, and fluorescence to infer such protein characteristics. Circular dichroism (CD) spectroscopy, the difference in absorption between circular polarized light, is a helpful technique when studying the percentage of secondary structures such as α-helices and β-sheets of a protein. Fluorescence, the emission of light, can be monitored during experiments where the protein becomes unfolded. The signal change of fluorescence during an unfolding curve using a chemical denaturant is presented here to determine the free energy between the folded and unfolded state of the model protein Cytochrome c.