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Schlagwörter:
Femtosecond;Crystallography;Carboxy-Myoglobin
Zusammenfassung:
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.
