Related Experiment Video
Updated: Jul 27, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
Observation of the cascaded atomic-to-global length scales driving protein motion
M R Armstrong1, J P Ogilvie, M L Cowan
1Department of Physics and Astronomy, University of Rochester, Bausch & Lomb Hall, Rochester, NY 14627-0171, USA.
Abstract:
Model studies of the ligand photodissociation process of carboxymyoglobin have been conducted by using amplified few-cycle laser pulses short enough in duration (<10 fs) to capture the phase of the induced nuclear motions. The reaction-driven modes are observed directly in real time and depict the pathway by which energy liberated in the localized reaction site is efficiently channeled to functionally relevant mesoscale motions of the protein.
More Related Videos
09:17Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
Published on: March 1, 2022
08:48High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Related Concept Videos
Protein Folding
Mechanical Protein Functions
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...