Phys. Rev. Lett. 100, 228103 (2008) [4 pages]Transient Protein Softening during the Working Cycle of a Molecular MachineReceived 13 December 2007; published 3 June 2008 Proper functioning of proteins usually requires a certain internal flexibility provided by stochastic structural fluctuations on the picosecond time scale. In contrast with conventional steady-state experiments, we report on a novel type of (laser-neutron) pump-probe experiment combining in situ activation of protein function with a time-dependent test of protein dynamics using quasielastic neutron scattering. A “transient protein softening” is shown to occur during the photocycle of bacteriorhodopsin as a direct proof for the functional significance of protein flexibility. © 2008 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.100.228103
DOI:
10.1103/PhysRevLett.100.228103
PACS:
87.16.dj, 87.14.ep, 87.15.hp
|
|
About | Terms and Conditions | Subscriptions | Search | Help
Use of the American Physical Society websites and journals implies that the user has read and agrees to our Terms and Conditions and any applicable Subscription Agreement. Physical Review®, Physical Review Letters®, Reviews of Modern Physics®, and Physical Review Special Topics® are trademarks of the American Physical Society.