Fast-Folding Kinetics Using Nanosecond Laser-Induced Temperature-Jump Methods

Michele Cerminara (1, 2)

1 Instituto IMDEA Nanociencia [Madrid]
2 Physique des fonctions biologiques / Physics of Biological Functions

The development of ultrafast kinetic methods is one of the factors that allowed the research on protein folding to flourish over the last twenty years. The introduction of new optical triggering techniques enabled to experimentally investigate the protein dynamics at the nanosecond to millisecond timescale, allowing researchers to test theoretical predictions and providing experimental benchmarks for computer simulations. In this work the details of how to perform kinetic experiments by the laserinduced temperature jump technique, using the two most commonly used probing techniques (namely infrared absorption and fluorescence spectroscopy) are given, with a strong emphasis on the practical details.

Mots clés: Protein Folding; Folding Kinetics; Pump and Probe; Temperature jump; Infrared absorption; Fluorescence; Förster Resonance Energy Transfer

Domaines: Sciences du Vivant [q-bio]; Biologie moléculaire

Michele Cerminara. Fast-Folding Kinetics Using Nanosecond Laser-Induced Temperature-Jump Methods. Protein Folding, 2376, Springer US, pp.117-134, 2022, Methods in Molecular Biology, 978-1-0716-1715-1. ⟨10.1007/978-1-0716-1716-8_6⟩. ⟨pasteur-04121260⟩