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Multidimensional photon correlation spectroscopy of cavity polaritons.

ABSTRACT: The strong coupling of atoms and molecules to radiation field modes in optical cavities creates dressed matter/field states known as polaritons with controllable dynamical and energy transfer properties. We propose a multidimensional optical spectroscopy technique for monitoring polariton dynamics. The response of a two-level atom to the time-dependent coupling to a single-cavity mode is monitored through time-and-frequency-resolved single-photon coincidence measurements of spontaneous emission. Polariton population and coherence dynamics and its variation with cavity photon number and controlled by gating parameters are predicted by solving the Jaynes-Cummings model.

SUBMITTER: Dorfman KE

PROVIDER: S-EPMC5816200 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Publications

Multidimensional photon correlation spectroscopy of cavity polaritons.

Dorfman Konstantin E KE Mukamel Shaul S

Proceedings of the National Academy of Sciences of the United States of America 20180131 7

The strong coupling of atoms and molecules to radiation field modes in optical cavities creates dressed matter/field states known as polaritons with controllable dynamical and energy transfer properties. We propose a multidimensional optical spectroscopy technique for monitoring polariton dynamics. The response of a two-level atom to the time-dependent coupling to a single-cavity mode is monitored through time-and-frequency-resolved single-photon coincidence measurements of spontaneous emission. ...[more]

PMID: 29386388

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Project description:Conformational motions of proteins are highly dynamic and intrinsically complex. To capture the temporal and spatial complexity of conformational motions and further to understand their roles in protein functions, an attempt is made to probe multidimensional conformational dynamics of proteins besides the typical one-dimensional FRET coordinate or the projected conformational motions on the one-dimensional FRET coordinate. T4 lysozyme hinge-bending motions between two domains along α-helix have been probed by single-molecule FRET. Nevertheless, the domain motions of T4 lysozyme are rather complex involving multiple coupled nuclear coordinates and most likely contain motions besides hinge-bending. It is highly likely that the multiple dimensional protein conformational motions beyond the typical enzymatic hinged-bending motions have profound impact on overall enzymatic functions. In this report, we have developed a single-molecule multiparameter photon stamping spectroscopy integrating fluorescence anisotropy, FRET, and fluorescence lifetime. This spectroscopic approach enables simultaneous observations of both FRET-related site-to-site conformational dynamics and molecular rotational (or orientational) motions of individual Cy3-Cy5 labeled T4 lysozyme molecules. We have further observed wide-distributed rotational flexibility along orientation coordinates by recording fluorescence anisotropy and simultaneously identified multiple intermediate conformational states along FRET coordinate by monitoring time-dependent donor lifetime, presenting a whole picture of multidimensional conformational dynamics in the process of T4 lysozyme open-close hinge-bending enzymatic turnover motions under enzymatic reaction conditions. By analyzing the autocorrelation functions of both lifetime and anisotropy trajectories, we have also observed the dynamic and static inhomogeneity of T4 lysozyme multidimensional conformational fluctuation dynamics, providing a fundamental understanding of the enzymatic reaction turnover dynamics associated with overall enzyme as well as the specific active-site conformational fluctuations that are not identifiable and resolvable in the conventional ensemble-averaged experiment.

Dataset Information

Multidimensional photon correlation spectroscopy of cavity polaritons.

Publications

Multidimensional photon correlation spectroscopy of cavity polaritons.

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