Abstract

The stabilisation of the structure of proteins in general and of collagen in particular, is produced through multiple weak interactions of a non-covalent nature, similar to those which take place within the medium in which it is placed. The degree of stabilisation of the protein structure will therefore be the result of the equilibrium between the internal interactions (within the protein) and the external ones which will take place with the components of the medium. The interactions of a hydrophobic character, that take place between non-polar regions of some molecules, have an important role in the stabilisation of the structure of the proteins. The nature of the hydrophobic effect has been the subject of numerous controversies. Apart from theoretical considerations, the importance of the hydrophobic effect in collagen has been evaluated experimentally by means of the study of the interaction with surfactants having a relatively simple and defined chemical structure. A mechanism, which takes account of the participation of forces of ionic and hydrophobic nature has been established for the total interaction process.