Proteins are the workhorses of living cells, providing essential functions such as structural support, signal transduction, enzymatic catalysis, transport and storage of small ligands. Atomic-resolution structures obtained with conventional X-ray crystallography show proteins essentially as static. In reality, however, proteins move and their motion is crucial for functioning. Although the structure and dynamics of proteins are intimately related, they are not equally well understood. A very large number of protein structures have been determined, but only a few studies have been able to monitor experimentally the dynamics of proteins in real time. In the last two decades, the availability of short (~100 ps) and intense (~109–1010 photons) X-ray pulses produced by third-generation synchrotrons have allowed the implementation of structural methods like time-resolved X-ray crystallography and time-resolved X-ray solution scattering that have allowed us to monitor protein motion in the nanosecond-to-millisecond timescale [1–4]. Time-resolved X-ray crystallography has been used to monitor processes such as the migration of a ligand from the protein active site to the surrounding solvent [5–7] or tertiary structural changes associated with allosteric transitions [8, 9]. On the other hand, time-resolved X-ray scattering in the so-called wide-angle X-ray scattering (WAXS) region  has been used to track conformational changes corresponding to large-amplitude protein motions such as the quaternary R-T transition of human hemoglobin [11–13], the relative motion of bacteriorhodopsin α-helices following retinal isomerization , or the open-to-close transition in bacterial phytochromes .
|Numero di pagine||5|
|Rivista||Synchrotron Radiation News|
|Stato di pubblicazione||Published - 2016|
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