Bacteriorhodopsin and the purple membrane of halobacteria

Mass spectrometric determination of the amino acid sequence of peptides and proteins

Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin

Steered molecular dynamics (SMD) induces unbinding of ligands and conformational changes in biomolecules on time scales accessible to molecular dynamics simulations. Time-dependent external forces are applied to a system, and the responses of the system are analyzed. SMD has already provided important qualitative insights into biologically relevant problems, as demonstrated here for applications ranging from identification of ligand binding pathways to explanation of elastic properties of proteins. First attempts to deduce potentials of mean force by discounting irreversible work performed on the system are summarized. The non-equilibrium statistical mechanics underlying analysis of SMD data is outlined.

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Steered Molecular Dynamics

Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2874%2981153-1

Reconstitution of bacteriorhodopsin

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2874%2981152-X

Lieselotte Schuhmann

Papers

Reconstitution of bacteriorhodopsin

Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: demonstration of an apo-membrane.