**Fourier Transform Infrared Spectroscopy in the Study of Hydrated Biological Macromolecules Fourier Transform Infrared Spectroscopy in the Study of Hydrated Biological Macromolecules**

Maria Grazia Bridelli Maria Grazia Bridelli

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Additional information is available at the end of the chapter Additional information is available at the end of the chapter

http://dx.doi.org/10.5772/66576

### **Abstract**

The interaction between biological macromolecules (proteins, nucleic acids, lipids and other biomolecules in the cell) and environmental water is an important determining factor in their conformational properties, stability and function. The hydration processes of biopolymers have been extensively studied in the past 20 years with reference to a considerable variety of models and concepts. In all recent works, a distinction is made between intracellular water that maintains the ordinary liquid state (bulk water) and water ordered in extended hydrogen‐bonded lattices at the surface and structured in the internal grooves of macromolecules (hydration water) in dependence on the chemical properties of the macromolecule surface. FTIR spectroscopy has been implemented in this field both for the sensitivity in the conformational analysis of biological macromol‐ ecules and the reliability in the investigation of the water network. A perturbation tech‐ nique such as dehydration‐rehydration treatment modifies the macromolecule structure and water distribution. It was applied to two structurally different proteins: lysozyme, a globular (α + β) protein and collagen, a fibrous protein characterized by the triple helix structure. Submitted to the treatment both of them display irreversible conformational changes.

**Keywords:** FTIR spectroscopy, biological macromolecules, hydration, adsorption isotherms, lysozyme, collagen
