Reconfigurable and real-time high-bandwidth Nyquist signal detection with low-bandwidth in silicon photonics.

We demonstrate for the first time, to the best of our knowledge, reconfigurable and real-time orthogonal time-domain detection of a high-bandwidth Nyquist signal with a low-bandwidth silicon photonics Mach-Zehnder modulator based receiver. As the Nyquist signal has a rectangular bandwidth, it can be multiplexed in the wavelength domain without any guardband as a part of a Nyquist-WDM superchannel. These superchannels can be additionally multiplexed in space and polarization.

Locking of microwave oscillators on the interharmonics of mode-locked laser signals.

In this paper, the theory of phase-locking of a microwave oscillator on the interharmonics, i.e. non-integer harmonics, of the repetition rate of the optical pulse train of a mode-locked laser (MLL) is developed.

Analysis of the effects of jitter, relative intensity noise, and nonlinearity on a photonic digital-to-analog converter based on optical Nyquist pulse synthesis.

An analysis of an optical Nyquist pulse synthesizer using Mach-Zehnder modulators is presented. The analysis allows to predict the upper limit of the effective number of bits of this type of photonic digital-to-analog converter. The analytical solution has been verified by means of electro-optic simulations.

Integrated source-free all optical sampling with a sampling rate of up to three times the RF bandwidth of silicon photonic MZM.

Source-free all optical sampling, based on the convolution of the signal spectrum with a frequency comb in an electronic-photonic, co-integrated silicon device will be presented for the first time, to the best of our knowledge. The method has the potential to achieve very high precision, requires only low power and can be fully tunable in the electrical domain. Sampling rates of three and four times the RF bandwidths of the photonics and electronics can be achieved.

Solubilization of proteins in aqueous two-phase extraction through combinations of phase-formers and displacement agents.

The aqueous two-phase extraction (ATPE) of therapeutic proteins is a promising separation alternative to cost-intensive chromatography, still being the workhorse of nowadays downstream processing. As shown in many publications, using NaCl as displacement agent in salt-polymer ATPE allows for a selective purification of the target protein immunoglobulin G (IgG) from human serum albumin (HSA, represents the impurity). However a high yield of the target protein is only achievable as long as the protein is stabilized in solution and not precipitated.

Novel Displacement Agents for Aqueous 2-Phase Extraction Can Be Estimated Based on Hybrid Shortcut Calculations.

The purification of therapeutic proteins is a challenging task with immediate need for optimization. Besides other techniques, aqueous 2-phase extraction (ATPE) of proteins has been shown to be a promising alternative to cost-intensive state-of-the-art chromatographic protein purification. Most likely, to enable a selective extraction, protein partitioning has to be influenced using a displacement agent to isolate the target protein from the impurities.

Protein partition coefficients can be estimated efficiently by hybrid shortcut calculations.

The extraction of therapeutic proteins like monoclonal antibodies in aqueous two-phase systems (ATPS) is a suitable alternative to common cost intensive chromatographic purification steps within the downstream processing. Thereby the protein partitioning can be selectively changed using a displacement agent (additional salt) in order to allow for a successful purification of the target protein. Within this work a new shortcut strategy for the calculation of protein partition coefficients in polymer-salt ATPS is presented.

Osmotic Virial Coefficients as Access to the Protein Partitioning in Aqueous Two-Phase Systems.

A promising alternative to state of the art chromatographic separations of therapeutic proteins is the extraction of the target protein using an aqueous two-phase system (ATPS). The use of an additional salt working as a displacement agent can influence the protein partitioning behavior in ATPS and thus enable a selective purification of the target protein. The selection of a suitable ATPS for protein extraction requires information concerning the protein-protein interactions (second osmotic virial coefficient B22 ) as well as the interactions between protein and solute (displacement agent and phase-forming components) (cross virial coefficient B23 ).