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Title: 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 (0.220–0.325 THz). The following proteins, ranging from low to high molecular weight, were chosen for this study: lysozyme, myoglobin, and bovine serum albumin (BSA). Absorption properties of solutions were studied at different concentrations of proteins ranging from 2 to 100 mg/ml. The concentration-dependent absorption of protein molecules was determined by treating the solution as a two-component model first; then, based on protein absorptivity, the extent of the hydration shell is estimated. Protein molecules are shown to possess a concentration-dependent absorptivity in water solutions. Absorption curves of all three proteins sharply peak towards a dilution-limit that is attributed to the enhanced flexibility of protein and amino acid side chains. An alternative approach to the determination of hydration shell thickness is thereby suggested, based on protein absorptivity. The proposed approach is independent of the absorption of the hydration shell. The derived estimate of hydration shell thickness for each protein supports previous findings that protein-water interaction dynamics extendsmore » beyond 2-3 water solvation-layers as predicted by molecular dynamics simulations and other techniques such as NMR, X-ray scattering, and neutron scattering. According to our estimations, the radius of the dynamic hydration shell is 16, 19, and 25 Å, respectively, for lysozyme, myoglobin, and BSA proteins and correlates with the dipole moment of the protein. It is also seen that THz radiation can serve as an initial estimate of the protein hydrophobicity.« less
Authors:
; ;  [1]
  1. School of Electronic Engineering and Computer Science, Queen Mary University of London, Mile End Road, London E1 4NS (United Kingdom)
Publication Date:
OSTI Identifier:
22416088
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Chemical Physics; Journal Volume: 142; Journal Issue: 5; Other Information: (c) 2015 Author(s); Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ABSORPTION; ABSORPTION SPECTROSCOPY; ABSORPTIVITY; ALBUMINS; AMINO ACIDS; AQUEOUS SOLUTIONS; CONCENTRATION RATIO; DILUTION; DIPOLE MOMENTS; HYDRATION; LAYERS; LYSOZYME; MOLECULAR DYNAMICS METHOD; MOLECULAR WEIGHT; MOLECULES; MYOGLOBIN; NEUTRON DIFFRACTION; NUCLEAR MAGNETIC RESONANCE; WATER; X-RAY DIFFRACTION