Protein energy landscapes determined by five-dimensional crystallography
Category
Published on
Type
journal-article
Author
Marius Schmidt and Vukica Srajer and Robert Henning and Hyotcherl Ihee and Namrta Purwar and Jason Tenboer and Shailesh Tripathi
Citation
Schmidt, M. et al., 2013. Protein energy landscapes determined by five-dimensional crystallography. Acta Crystallogr D, 69(12), pp.2534–2542. Available at: http://dx.doi.org/10.1107/s0907444913025997.
Abstract
Free-energy landscapes decisively determine the progress of enzymatically catalyzed reactions [Cornish-Bowden (2012),Fundamentals of Enzyme Kinetics, 4th ed.]. Time-resolved macromolecular crystallography unifies transient-state kinetics with structure determination [Moffat (2001),Chem. Rev.101, 1569–1581; Schmidtet al.(2005),Methods Mol. Biol.305, 115–154; Schmidt (2008),Ultrashort Laser Pulses in Medicine and Biology] because both can be determined from the same set of X-ray data. Here, it is demonstrated how barriers of activation can be determined solely from five-dimensional crystallography, where in addition to space and time, temperature is a variable as well [Schmidtet al.(2010),Acta Cryst.A66, 198–206]. Directly linking molecular structures with barriers of activation between them allows insight into the structural nature of the barrier to be gained. Comprehensive time series of crystallographic data at 14 different temperature settings were analyzed and the entropy and enthalpy contributions to the barriers of activation were determined. One hundred years after the discovery of X-ray scattering, these results advance X-ray structure determination to a new frontier: the determination of energy landscapes.
DOI
Funding
NSF-STC Biology with X-ray Lasers (NSF-1231306)
