Related Experiment Video
Updated: Jun 20, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
Published on: January 5, 2024
Single-molecule protein interaction conformational dynamics
1Department of Chemistry, Center for Photochemical Sciences, Bowling Green State University, Bowling Green, OH 43403, USA. hplu@bgsu.edu
Abstract:
Protein conformational fluctuations and dynamics, often associated with static and dynamic inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such spatially and temporally inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins involve in a multiple-step and multiple-conformation complex chemical interactions and transformations, such as in protein-protein interactions and protein-DNA interactions. Single-molecule spectroscopy is a powerful approach to analyze protein conformational dynamics under physiological conditions, providing dynamic perspectives on a molecular-level understanding of protein structure-function mechanisms.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein-protein Interfaces
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Intrinsically Disordered Proteins

