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Capturing Functionally Relevant Protein Motions at the Atomic Level: Femtosecond Time Resolved Serial Crystallography of Ligand Dissociation of Carboxy-Myoglobin

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Marx,  Alexander
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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Epp,  Sascha W.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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Miller,  R. J. Dwayne
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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Citation

Müller-Werkmeister, H. M., Kuo, A., Ginn, H. M., Oghbaey, S., Sarracini, A., Pare-Labrosse, O., et al. (2016). Capturing Functionally Relevant Protein Motions at the Atomic Level: Femtosecond Time Resolved Serial Crystallography of Ligand Dissociation of Carboxy-Myoglobin. Biophysical Journal, 110(3), 513a. doi:10.1016/j.bpj.2015.11.2745.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-44F7-B
Abstract
The recent advent of X-Ray free electron lasers with highest brilliance and femtosecond pulses opens new possibilities for time-resolved protein crystallography [Miller, R.J.D, Science, 2014, 343, 1108-1116]. A fundamental biophysical question becomes accessible experimentally now: The investigation of protein dynamics with all atomic resolution on the shortest biochemically relevant timescale around 100 fs. Here is where bond-breaking events occur, which in turn translate into secondary and tertiary structure changes and cause a protein to fulfill its function over a wide range of timescales.