Crystal structure of CobK reveals strand-swapping between Rossmann-fold domains and molecular basis of the reduced precorrin product trap.

CobK catalyzes the essential reduction of the precorrin ring in the cobalamin biosynthetic pathway. The crystal structure of CobK reveals that the enzyme, despite not having the signature sequence, comprises two Rossmann fold domains which bind coenzyme and substrate respectively. The two parallel β-sheets have swapped their last β-strands giving a novel sheet topology which is an interesting variation on the Rossmann-fold.

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected.

The initial purpose of the study is to systematically investigate the solvation properties of different proteins in water solution by terahertz (THz) radiation absorption. Transmission measurements of protein water solutions have been performed using a vector network analyser-driven quasi-optical bench covering the WR-3 waveguide band (0.220-0.

Terahertz spectral domain computational analysis of hydration shell of proteins with increasingly complex tertiary structure.

Solvation dynamics of biomolecules and water in a hydration shell have been studied by different methods; however, a clear picture of this process is not yet established. Terahertz (THz) studies of molecular behavior in binary solutions present unique information on the picosecond motions of molecules. A complete mechanical interpretation of THz absorption spectra associated with solvated biomolecules remains a challenging task.

Revised metrology for enhanced accuracy in complex optical constant determination by THz-time-domain spectrometry.

THz time-domain spectrometry (TDS) probes the complex polarization response of materials. Various analytical procedures are applied by many to extract the associated material optical constants. This has commonly been done by iteratively varying material parameters in order to achieve a match between experiment and a theoretical transfer function (TF).