Martina Havenith

TL;DR: It is shown here that Terahertz spectroscopy directly probes such solvation dynamics around proteins, and determines the width of the dynamical hydration layer, and investigates the dependence ofsolvation dynamics on protein concentration.

TL;DR: A review of the experimental and computational advances over the past decade in understanding the role of water in the dynamics, structure, and function of proteins focuses on the combination of X-ray and neutron crystallography, NMR, terahertz spectroscopy, mass spectroscopic, thermodynamics, and computer simulations to reveal how water assist proteins in their function.

TL;DR: This result provides a molecular mechanism explaining the experimentally determined sensitivity of absorption changes in the THz domain in terms of distinct, solute-induced dynamical properties in solvation shells of (bio)molecules—even in the absence of well-defined resonances.

TL;DR: The present study demonstrates that terahertz spectroscopy is a sensitive tool to detect solute-induced changes in the water network and is shown to probe the collective modes in theWater network.

TL;DR: Nitrogen-containing functional groups were generated on the surface of partially oxidized multi-walled carbon nanotubes (CNTs) via post-treatment in ammonia via high-resolution X-ray photoelectron spectroscopy (XPS) and temperature-programmed desorption (TPD).