Time-Resolved X-Ray Crystallography of Heme Proteins
Heme proteins, with their natural photosensitivity, are excellent systems for the application of time-resolved crystallographic methods. Ligand dissociation can be readily initiated by a short laser pulse with global structural changes probed at the atomic level by X-rays in real time. Third-generation synchrotrons provide 100-ps X-ray pulses of sufficient intensity for monitoring very fast processes. Successful application of such time-resolved crystallographic experiments requires that the structural changes being monitored are compatible with the crystal lattice. These techniques have recently permitted observing for the first time allosteric transitions in real time for a cooperative dimeric hemoglobin.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1006586
- Journal Information:
- Methods Enzymol., Vol. 437, Issue 2008; ISSN 0076-6879
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Cooperative protein structural dynamics of homodimeric hemoglobin linked to water cluster at subunit interface revealed by time-resolved X-ray solution scattering
[An experiment in time-resolved step-scan FT-IR for use in dynamic photophysical studies of cytochrome-C oxidase and other heme proteins]. Final report