Related Experiment Video
Updated: Oct 1, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Time-resolved FTIR difference spectroscopy as tool for investigating refolding reactions of ribonuclease T1
Ralf Moritz1, Diane Reinstädler, Heinz Fabian
1Robert Koch-Institut, P34, Nordufer 20, 13353 Berlin, Germany. ralf.moritz@gmx.de
Abstract:
The structurally well-characterized enzyme ribonuclease T1 was used as a model protein to further evaluate time-resolved Fourier transform IR difference spectroscopy in conjunction with temperature-jump techniques as a useful detection technique for protein folding studies. Compared to the wild-type protein, it was confirmed that the lack of one cis-proline bond at position 55 of the S54G/P55N variant is sufficient to significantly simplify and accelerate the refolding process. This result was sustained by the characterization of the early refolding events that occurred within the experimental dead time.
Related Concept Videos
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
Total Internal Reflection Fluorescence Microscopy
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...

