Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.
We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.
Cammarata
Marco
M
European Synchrotron Radiation Facility, Grenoble Cedex 38043, BP 220, France. marco.cammarata@esrf.eu
Levantino
Matteo
M
Schotte
Friedrich
F
Anfinrud
Philip A
PA
Ewald
Friederike
F
Choi
Jungkweon
J
Cupane
Antonio
A
Wulff
Michael
M
Ihee
Hyotcherl
H
D018360:Crystallography, X-Ray; D045304:Cytochromes c / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D012542:Scattering, Radiation; D012680:Sensitivity and Specificity; D014965:X-Rays
D006454:Hemoglobins; D009211:Myoglobin; D045304:Cytochromes c