Data Analysis for Time-Resolved QENS Experiments in Biophysics

TL;DR

This paper presents a method combining time-resolved quasielastic neutron scattering with laser activation to analyze protein dynamics in bacteriorhodopsin, revealing hydration effects but consistent laser responses.

Contribution

It introduces a novel experimental approach for studying protein dynamics with time resolution and in situ activation in biophysics.

Findings

Water content influences QENS spectra lineshapes.

Laser-induced response remains consistent across samples.

Hydration level affects internal protein dynamics.

Abstract

To study the correlation between internal protein dynamics and protein functionality of bacteriorhodopsin, we have performed time-resolved quasielastic neutron scattering (QENS) experiments combined with in situ laser activation of protein function. A set of purple membrane samples with different lamellar lattice constants and, hence, different hydration levels has been examined at different time delays between the laser and neutron pulses. While the water content affected the lineshapes of QENS spectra, the laser-induced response remained constant within the accuracy of the method.