Pushing Boundaries In Protein Structure-Function Analysis: How MMS Exceeds CD Spectroscopy At In-Situ Detection And Characterization Of Structural Changes In Proteins

Circular Dichroism (CD) spectroscopy is a common method for determining protein secondary structure, especially for helix-rich proteins, but it faces significant challenges with other structural motifs like beta-sheets and unordered regions. This is due to overlapping signals and the much stronger alpha-helical signal, which can distort deconvolution.

In contrast, Microfluidic Modulation Spectroscopy (MMS) has proven to be a robust and sensitive tool, capable of detecting subtle structural changes as low as 0.76%, with well-separated and similarly-magnitude signals for various motifs. This study directly compares MMS and CD spectroscopy in analyzing a concentration-dependent oligomerization mechanism of a beta-sheet-rich protein, revealing MMS's superior ability to capture these critical structural shifts. Learn why MMS is the preferred method for complex protein analysis. Download the application note to learn more.