Denaturation research needs

Urea is an important cosolvent generally used in the study of denaturation processes in several proteins. Inspired by the need to understand the microscopic basis of the mechanism of protein denaturation, researchers have performed MD simulations to assess the effects of urea on the hydrophobic interaction between two methane molecules. 

Actomyosin denatures also in situ under the influence of hypertonic salt solutions. When cod muscle is immersed in various concentrations of sodium chloride, there is a critical salt content in the fillet (8% to 10% NaCl) at which denaturation occurs together with a rapid loss of water and uptake of salt (Duerr and Dyer, 1952 Fougere, 1952). In herring, however, this critical salt concentration is much lower (3 % NaCl) (Nikkila and Linko, 1954b). The stability of the native configuration appears very variable, but we are unable to explain such differences. The need for a better knowledge of the protein itself is clearly stressed by these researches. Let us now consider the recent progress made in this direction. 

Many polymeric materials used in biomedical research are biohybrids, meaning a combination of synthetic polymers and biological macromolecules. In addition, the interaction of a biomacromolecule like a peptide and any synthetic polymer is of high interest for potential application, for example, if there are conformational changes or denaturation of the proteins in contact with a polymeric surface and, thus, specific characterization tools not only for the synthetic polymers are of need but also for biomacromolecules. Therefore, in the following, specific techniques are described for the characterization of polypeptides as an example for a typical biological macromolecule. 

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