Time-resolved x-ray solution scattering from detergent solubilized visual rhodopsin
Year: 2026
Type: article
Abstract: Time-resolved x-ray solution scattering (TR-XSS) studies provide experimental probes of transient conformational states in macromolecules. Difference x-ray scattering curves from integral membrane proteins are predicted to be influenced by the presence of the surrounding detergent micelle. Here, we present time-dependent x-ray solution scattering data from visual rhodopsin when solubilized in two different detergents: the nonionic surfactant n-dodecyl-β-D-maltoside and the zwitterionic detergent 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate. Both detergents produce micelles that surround rhodopsin, yet they have different composition, density and critical micelle concentrations and yield different x-ray scattering properties. Our theoretical framework is able to fit the experimental TR-XSS data for photoactivated rhodopsin in both detergents, yielding experimental verification of how x-ray scattering contrast from the detergent molecules influences difference x-ray scattering measurements from integral membrane proteins. These results increase confidence when modeling conformational changes of integral membrane proteins from an ensemble of predicted structures.
Source: Biophysical Journal
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,000
Awards: Light-Induced Protein Quake of Visual Rhodopsin Investigated by Femtosecond Time-Resolved X-Ray Scattering, Collaborative Research: Emergent Dynamics and Scaling Laws in Bioinspired Lipid Membranes, Protein and cellular structural dynamics, Analyzing protein dynamics in receptor signaling relevant to pharmacology, G5309289743, Essential Role of Water and Lipids in G-Protein-Coupled Receptor Chemistry
OpenAlex ID: W7120119687
