Abstract
Here we report sub-100-ps structural dynamics of horse heart myoglobin revealed by time-resolved X-ray solution scattering. By applying the time-slicing scheme to the measurement and subsequent deconvolution, we investigate the protein structural dynamics that occur faster than the X-ray temporal pulse width of synchrotrons (∼100 ps). The singular value decomposition analysis of the experimental data suggests that two structurally distinguishable intermediates are formed within 100 ps. In particular, the global structural change occurring on the time scale of 70 ps is identified.
Original language | English |
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Pages (from-to) | 137-142 |
Number of pages | 6 |
Journal | Chemical Physics |
Volume | 442 |
DOIs | |
State | Published - 17 Oct 2014 |
Bibliographical note
Publisher Copyright:© 2014 Elsevier B.V. All rights reserved.
Keywords
- Myoglobin
- Structural dynamics
- Time-resolved X-ray solution scattering
- Time-slicing