RosettaHDX: Predicting antibody-antigen interaction from hydrogen-deuterium exchange mass spectrometry data.

High-throughput characterization of antibody-antigen complexes at the atomic level is critical for understanding antibody function enabling therapeutic development. Hydrogen-deuterium exchange mass spectrometry (HDX-MS) enables rapid epitope mapping, but its data are too sparse for independent structure determination. In this study, we introduce RosettaHDX, a hybrid method that combines computational docking with differential HDX-MS data to enhance the accuracy of antibody-antigen complex models beyond what either method can achieve individually.

The NADH-dependent flavin reductase ThdF follows an ordered sequential mechanism though crystal structures reveal two FAD molecules in the active site.

Two-component flavin-dependent monooxygenases are of great interest as biocatalysts for the production of pharmaceuticals and other relevant molecules, as they catalyze chemically important reactions such as hydroxylation, epoxidation and halogenation. The monooxygenase components require a separate flavin reductase, which provides the necessary reduced flavin cofactor. The tryptophan halogenase Thal from Streptomyces albogriseolus is a well-characterized two-component flavin-dependent halogenase.

Sparse-deconvolution terahertz near-field microprobe tomography enabling non-destructive inspection of small solid dosage forms.

Terahertz (THz) pulsed imaging is a powerful tool for investigating solid dosage forms. However, traditional far-field systems struggle with physically small samples and strongly bent surfaces due to inherently limited lateral resolution. The present study introduces a novel approach using photo-conductive near-field microprobes (PC-NFMs) with a THz time-domain spectroscopy module to overcome the limitations of far-field setups concerning their achievable lateral resolution.