Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein.

ABSTRACT: Femtosecond time-resolved crystallography (TRC) on proteins enables resolving the spatial structure of short-lived photocycle intermediates. An open question is whether confinement and lower hydration of the proteins in the crystalline state affect the light-induced structural transformations. Here, we measured the full photocycle dynamics of a signal transduction protein often used as model system in TRC, Photoactive Yellow Protein (PYP), in the crystalline state and compared those to the dynamics in solution, utilizing electronic and vibrational transient absorption measurements from 100 fs over 12 decades in time. We find that the photocycle kinetics and structural dynamics of PYP in the crystalline form deviate from those in solution from the very first steps following photon absorptio

SUBMITTER: Konold PE 

PROVIDER: S-EPMC7447820 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature