Related Experiment Video
Updated: Jun 29, 2026

Direct Imaging of Laser-driven Ultrafast Molecular Rotation
Published on: February 4, 2017
Direct observation of correlated interdomain motion in alcohol dehydrogenase
Ralf Biehl1, Bernd Hoffmann, Michael Monkenbusch
1Institut für Festkörperforschung, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Abstract:
Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.
More Related Videos
06:48Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
Published on: January 5, 2024
10:03Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Related Concept Videos
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
IR and UV–Vis Spectroscopy of Aldehydes and Ketones
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
¹H NMR of Labile Protons: Temporal Resolution
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...