Speaker
Description
Light is an important stimulus for many biological processes. While structural changes in photo-responsive proteins are studied using well-established techniques, the implications of dynamic transitions during the photo-switching process remain to be assessed. High-resolution neutron backscattering spectroscopy enables the study of protein dynamics on the pico- to nanosecond timescale.
In this contribution, the photocycle of the pP-SB1-LOV protein is investigated using neutron backscattering spectroscopy on two instruments: the IRIS time-of-flight inverted-geometry crystal analyser and the IN16B high-resolution backscattering spectrometer.
Experiments were conducted initially with ex-situ illumination, and later with in-situ illumination, to observe the dynamics of the stationary dark-adapted and illuminated states. Comparisons are drawn between the quasi-elastic neutron scattering (QENS) observables and QENS observables derived from molecular dynamics simulations using the MDANSE software package of these stationary states. Further, the dynamic transitions along the dark-recovery process were observed by fixed window scans as well as continuous QENS spectra.
Resolving the dynamics of photo-responsive proteins throughout their photocycle within the constraints of a neutron backscattering experiment demands careful consideration of experimental design and data analysis framework, which will be continued in a long-term proposal aiming to develop pump-probe experiments at IN16B.
| Session | Biology/Health |
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