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

Magnus Andersson (Institutionen för kemi- och bioteknik, Molekylär mikroskopi) ; J. Vincent ; David van der Spoel ; Jan Davidsson ; Richard Neutze
Structure (0969-2126). Vol. 16 (2008), 1, p. 21-28.
[Artikel, refereegranskad vetenskaplig]

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.

Denna post skapades 2008-10-30. Senast ändrad 2016-08-16.
CPL Pubid: 76649


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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Molekylär mikroskopi (2008-2014)
Institutionen för kemi (2001-2011)



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Visualizing structural dynamics: from small molecules to membrane proteins