Solution X-ray scattering (S/WAXS) and structure formation in protein dynamics

TL;DR

This paper introduces a novel approach combining mean field theory and Glauber algorithm to interpret S/WAXS data for protein dynamics, providing accurate analysis over various temperatures and predicting future experimental outcomes.

Contribution

It develops a new methodology integrating mean field theory with Glauber algorithm for analyzing protein structure formation in S/WAXS experiments, demonstrated on the Engrailed homeodomain protein.

Findings

Accurate interpretation of S/WAXS data over extended temperature ranges.

Predictions of scattering behavior at different ambient temperatures.

Comparison showing advantages over all-atom molecular dynamics simulations.

Abstract

We propose to develop mean field theory in combination with Glauber algorithm, to model and interpret protein dynamics and structure formation in small to wide angle x-ray scattering (S/WAXS) experiments. We develop the methodology by analysing the Engrailed homeodomain protein as an example. We demonstrate how to interpret S/WAXS data with a good precision and over an extended temperature range. We explain experimentally observed phenomena in terms of protein phase structure, and we make predictions for future experiments how the scattering data behaves at different ambient temperature values. We conclude that a combination of mean field theory with Glauber algorithm has the potential to develop into a highly accurate, computationally effective and predictive tool for analysing S/WAXS data. Finally, we compare our results with those obtained previously in an all-atom molecular dynamics simulation.