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Updated: Oct 20, 2025

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Multiscale conformational dynamics probed by time-resolved circular dichroism from seconds to picoseconds
François Hache1, Pascale Changenet1
1Optics and Biosciences Laboratory, CNRS, INSERM, Ecole Polytechnique, Institut Polytechnique de Paris, Palaiseau, France.
Time-resolved circular dichroism (TRCD) probes molecular dynamics across diverse timescales. Our advancements enable studying rapid pico-nanosecond events and slower protein/DNA folding processes with high temporal resolution.
Area of Science:
- Biophysical Chemistry
- Molecular Spectroscopy
- Protein Dynamics
Background:
- Time-resolved circular dichroism (TRCD) is a powerful technique for observing ultrafast molecular transformations.
- Investigating conformational changes in biomolecules requires methods with high temporal resolution.
- Previous TRCD studies have explored various molecular systems and processes.
Purpose of the Study:
- To present an overview of global advancements in time-resolved circular dichroism.
- To showcase novel experimental setups developed for TRCD.
- To demonstrate the application of TRCD across a wide range of timescales, from picoseconds to seconds.
Main Methods:
- Development of advanced experimental setups for time-resolved circular dichroism.
- Application of TRCD to study local phenomena in molecular systems.
- Utilizing TRCD to investigate slow conformational changes in proteins and DNA folding.
Main Results:
- TRCD instrumentation has evolved significantly over decades.
- Novel experimental designs allow for pico-nanosecond to second-scale investigations.
- Emblematic experiments highlight the versatility of TRCD in studying molecular dynamics.
Conclusions:
- TRCD is a versatile spectroscopic tool for molecular dynamics.
- Our developed methodologies extend the accessible timescale for TRCD studies.
- TRCD provides insights into both rapid local events and slow biomolecular processes like folding.
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