The biological function of many macromolecules such as proteins and RNA are tightly coupled to their conformation and their conformational dynamic. The correct folding of a protein into its native state is essential for its biological function. Misfolded or unfolded proteins are known to be either (partially) inactive or to even display toxic functionality. Studying how proteins fold correctly and undergo conformational changes is therefore crucial to understand the underlying biological mechanism and how diseases arise. Single-molecule Force Spectroscopy (SMFS) represents an ideal tool to study these molecular phenomena because of their unique capability to isolate individual biomolecules and observe conformational transitions and unfolding processes as they happen in real-time.
The Protein folding Application Note explains how LUMICKS’ C-Trap® technology allows for multi-domain protein unfolding steps to be studied, and enables the visualization of relative domain positions using FRET.
Read the Application note here.
