Related Experiment Video
Updated: Nov 15, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
Dynamical spectroscopy and microscopy of proteins in cells
Martin Gruebele1, Gary J Pielak2
1Department of Chemistry, Department of Physics, and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Understanding protein folding in cells is advancing rapidly. New research reveals protein surfaces are key regulators of protein mobility, function, and interactions within the cellular environment.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- A robust understanding of protein folding is established.
- The influence of the in-cell environment on protein dynamics remains an active area of investigation.
Purpose of the Study:
- To review recent advancements in studying fast in-cell protein dynamics.
- To discuss the emerging role of protein surfaces in cellular processes.
Main Methods:
- In-cell Nuclear Magnetic Resonance (NMR) spectroscopy.
- Time-resolved fluorescence microscopies.
Main Results:
- Recent studies have accelerated the understanding of protein dynamics on the nanosecond to second timescale within cells.
- Protein surfaces are increasingly recognized for their roles beyond solvent interaction.
Conclusions:
- In-cell environments significantly modulate protein folding, binding, and function.
- Protein surfaces act as critical cellular components controlling protein mobility, function, and interactions, including post-translational modifications.
More Related Videos
10:03Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
14:12Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
Published on: December 11, 2021
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...
Studying the Cytoskeleton
Two-Dimensional Microscopy in Microbiology
Protein Diffusion in the Membrane