7 Protein–Ligand Interaction Probed (2009)
Time-resolved Crystallography, Marius Schmidt, Hyotcherl Ihee, Reinhard Pahl, Vukica Srajer
Time-resolved (TR) crystallography is a unique method for determining the structures of intermediates in biomolecular reactions. The technique reached its mature stage with the development of the...
Knapp, James E., Pahl, Reinhard, Srajer, Vukica, Royer, William E.
Protein allostery provides mechanisms for regulation of biological function at the molecular level. We present here an investigation of global, ligand-induced allosteric transition in a protein by...
Protein kinetics: Structures of intermediates and reaction mechanism from time-resolved x-ray data
Schmidt, Marius, Pahl, Reinhard, Srajer, Vukica, Anderson, Spencer, Ren, Zhong, Ihee, Hyotcherl, ...
We determine the number of authentic reaction intermediates in the later stages of the photocycle of photoactive yellow protein at room temperature, their atomic structures, and a consistent set of...
Baxter, Richard H. G., Ponomarenko, Nina, Šrajer, Vukica, Pahl, Reinhard, Moffat, Keith, Norris, James R.
Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly...
Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds
Ihee, Hyotcherl, Rajagopal, Sudarshan, Šrajer, Vukica, Pahl, Reinhard, Anderson, Spencer, Schmidt, Marius, ...
Determining 3D intermediate structures during the biological action of proteins in real time under ambient conditions is essential for understanding how proteins function. Here we use time-resolved...
Schmidt, Marius, Nienhaus, Karin, Pahl, Reinhard, Krasselt, Angela, Anderson, Spencer, Parak, Fritz, ...
By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin (Mb) mutant L29W from nanoseconds to seconds after...
Knapp, James E., Pahl, Reinhard, Šrajer, Vukica, Royer, William E.
Protein allostery provides mechanisms for regulation of biological function at the molecular level. We present here an investigation of global, ligand-induced allosteric transition in a protein by...
Protein kinetics: Structures of intermediates and reaction mechanism from time-resolved x-ray data
Schmidt, Marius, Pahl, Reinhard, Srajer, Vukica, Anderson, Spencer, Ren, Zhong, Ihee, Hyotcherl, ...
We determine the number of authentic reaction intermediates in the later stages of the photocycle of photoactive yellow protein at room temperature, their atomic structures, and a consistent set of...
Baxter, Richard H. G., Ponomarenko, Nina, Šrajer, Vukica, Pahl, Reinhard, Moffat, Keith, Norris, James R.
Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly...
Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds
Ihee, Hyotcherl, Rajagopal, Sudarshan, Šrajer, Vukica, Pahl, Reinhard, Anderson, Spencer, Schmidt, Marius, ...
Determining 3D intermediate structures during the biological action of proteins in real time under ambient conditions is essential for understanding how proteins function. Here we use time-resolved...
Schmidt, Marius, Nienhaus, Karin, Pahl, Reinhard, Krasselt, Angela, Anderson, Spencer, Parak, Fritz, ...
By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin (Mb) mutant L29W from nanoseconds to seconds after...
Knapp, James E., Pahl, Reinhard, Šrajer, Vukica, Royer, William E.
Protein allostery provides mechanisms for regulation of biological function at the molecular level. We present here an investigation of global, ligand-induced allosteric transition in a protein by...