The miniaturization of polarization beam splitters(PBSs) is vital for ultradense chip-scale photonic integrated circuits. However, the small PBSs based on complex hybrid plasmonic structures exhibit large fabrication difficulties or high insertion losses. Here, by designing a bending multimode plasmonic waveguide, an ultrabroadband on-chip plasmonic PBS with low insertion losses is numerically and experimentally realized. The multimode plasmonic waveguide, consisting of a metal strip with a V-shaped groove on the metal surface, supports the symmetric and antisymmetric surface plasmon polariton(SPP) waveguide modes in nature. Due to the different field confinements of the two SPP waveguide modes, which result in different bending losses, the two incident SPP waveguide modes of orthogonal polarization states are efficiently split in the bending multimode plasmonic waveguide. The numerical simulations show that the operation bandwidth of the proposed PBS is as large as 430 nm because there is no resonance or interference effect in the splitting process. Compared with the complex hybrid plasmonic structure, the simple bending multimode plasmonic waveguide is much easier to fabricate. In the experiment, a broadband(Δλ≈ 120 nm) and low-insertion-loss(<3 dB with a minimum insertion loss of 0.7 dB) PBS is demonstrated by using the strongly confined waveguide modes as the incident sources in the bending multimode plasmonic waveguide.
Internal solvation of protein was studied by site-directed mutagenesis, with which an intrinsically fluorescent probe,tryptophan, is inserted into the desired position inside a protein molecule for ultrafast spectroscopic study. Here we review this unique method for protein dynamics research. We first introduce the frontiers of protein solvation, site-directed mutagenesis, protein stability and characteristics, and the spectroscopic methods. Then we present time-resolved spectroscopic dynamics of solvation dynamics inside cavities of active sites. The studies are carried out on a globular protein, staphylococcal nuclease. The solvation at sites inside the protein molecule＇s cavities clearly reveals characteristics of the local environment. These solvation behaviors are directly correlated to enzyme activity.
