A Proposed Time-Resolved X-Ray Scattering Approach to Track Local and Global Conformational Changes in Membrane Transport Proteins
Journal article, 2008

Time-resolved X-ray scattering has emerged as a powerful technique for studying the rapid structural dynamics of small molecules in solution. Membrane-protein-catalyzed transport processes frequently couple large-scale conformational changes of the transporter with local structural changes perturbing the uptake and release of the transported substrate. Using light-driven halide ion transport catalyzed by halorhodopsin as a model system, we combine molecular dynamics simulations with X-ray scattering calculations to demonstrate how small-molecule time-resolved X-ray scattering can be extended to the study of membrane transport processes. In particular, by introducing strongly scattering atoms to label specific positions within the protein and substrate, the technique of time-resolved wide-angle X-ray scattering can reveal both local and global conformational changes. This approach simultaneously enables the direct visualization of global rearrangements and substrate movement, crucial concepts that underpin the alternating access paradigm for membrane transport proteins.

Author

Magnus Andersson

Chalmers, Chemical and Biological Engineering, Molecular Imaging

J Vincent

Uppsala University

David van der Spoel

Uppsala University

J Davidsson

Uppsala University

Richard Neutze

University of Gothenburg

Structure

0969-2126 (ISSN)

Vol. 16 1 21-28

Subject Categories

Structural Biology

Chemical Sciences

DOI

10.1016/j.str.2007.10.016

PubMed

18184580

More information

Latest update

2/28/2018