Length-scale dependence of protein hydration-shell density

An increase in protein hydration-shell density relative to that of the bulk is observed (in the range of 4–14%) for all studied proteins and this density-increment, which decreases for decreasing protein size, is caused by the protein size only.

Germanium Plasmon Enhanced Resonators for Label-Free Terahertz Protein Sensing

A Terahertz protein sensing concept based on subwavelength Ge resonators is presented. Ge bowtie resonators, compatible with CMOS fabrication technology, have been designed and characterized with a resonance frequency of 0.5 THz and calculated local intensity enhancement of 10.000. Selective biofunctionalization of Ge resonators on Si wafer was achieved in one step using lipoic acid-HaloTag ligand (LA-HTL) for biofunctionalization and passivation. The results lay the foundation for future investigation of protein tertiary structure and the dynamics of protein hydration shell in response to protein conformation changes.

The unfolding effects on the protein hydration shell and partial molar volume: a computational study

In this paper we apply the computational analysis recently proposed by our group to characterize the solvation properties of a native protein in aqueous solution, and to four model aqueous solutions of globular proteins in their unfolded states thus characterizing the protein unfolded state hydration shell and quantitatively evaluating the protein unfolded state partial molar volumes.