Raman spectroscopy hydrated proteins

The cornea accounts for about 70% of the refractive power of the unaccommodated human eye, and therefore plays an important role in maintaining optimal vision. Apart from water, the cornea consists of 15% collagen proteins, which are mostly comprised of glycine, an aliphatic amino acid, and proline, the only cyclic amino acid. Areas where Raman spectroscopy can contribute include investigations of collagen proteins, corneal hydration status, and the pharmacokinetics of topically applied ocular hydration drugs. 

The IR and Raman spectra of partially hydrated proteins are a rich source of fundamental information on both water and protein species, owing to the sensitivity of vibrational modes to hydrogen bonding. The similar chemistry of water—water and water—peptide interactions requires that there be great accuracy in spectroscopic measurements of the hydration process. Since the review of the field by Kuntz and Kauz-mann (1974), the Fourier transform technique for IR and the tunable laser for Raman spectroscopy have offered important improvements in methodology. 

Protein dynamics, as a function of hydration, 191 Raman spectroscopy, and electrolytic solutions. 

Hydration is so important for the structural, physical and biological properties of the proteins, that it has been studied by a variety of methods such as Raman, IR and NMR spectroscopy, calorimetry, gravimetry, molecular dynamics [621, 622, 810, 827-834]. 

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