Protein Folding and Conformational Changes

Today’s scientific trends are racing towards smaller scales and experimentation that provides both structural and mechanistic insights. To decipher protein structure and function you need methods capable of studying how proteins fold correctly and undergo conformational changes to accomplish their biological function. We offer solutions that enable you to measure, manipulate and visualize protein folding and unfolding, with both high throughput and resolution.

Study Protein Folding and Conformational Dynamics at the Nanoscale

with: Optical Tweezers and Fluorescence Microscopy

Scientists can use optical tweezers to trap beads and catch a biomolecule, such as a protein, in between. The folding and unfolding of the protein can then be monitored by moving the beads while measuring the force and extension. The combination of optical tweezers with simultaneous multicolor fluorescence measurements (e.g. with FRET) allows correlating the global mechanical properties of the protein with the local structural properties. With optical tweezers – fluorescence microscopy you can:

Investigate protein folding and unfolding in real time, at the single molecule level and with high resolution
Measure highly detailed equilibrium dynamics over long periods of time to identify the protein (un)folding pathway and map the energy landscape
Correlate global mechanical properties of the protein with local structural properties
Perform experiments under biologically relevant conditions and highly crowded environments and link the in vitro experiment with the in vivo situation
Study the effect of small molecules and biologics in protein structure and dynamics.

View Detailed Application

Learn more about:

Technology
Optical Tweezers and Fluorescence Microscopy

Measure Protein Folding and Conformational Dynamics with High Throughput

with: Parallel Single-Molecule Force Spectroscopy

Scientists can use acoustic forces to manipulate, stretch and measure hundreds of single molecules at the same time. Multiple proteins can be tethered between a bead and a glass surface. Using Acoustic Force Spectroscopy (AFS) technology you can then apply controlled forces on all beads synchronously and probe the mechanical properties of each protein in parallel. With this highly parallel single-molecule method you can:

Investigate how multiple proteins fold and unfold in real time, at the single molecule level with high throughput
Measure equilibrium dynamics over long periods of time to identify the protein (un)folding pathway and map the energy landscape
Perform experiments under biologically relevant conditions and link the in vitro experiment with the in vivo situation
Study the effect of small molecules and biologics in protein structure, and
Receive large datasets containing many single-molecule measurements from a single experiment.