Denatured proteins research interest

Pauling s protein model was not the only one generating interest during the 1930s. The same year that he and protein researcher Alfred Mirsky published their ideas on denaturation, a brilliant and unconventional British scientist gained worldwide attention with her own, very different, ideas about proteins. 

There is a continuing interest to improve and extend the fimctional properties range of dairy proteins to provide both health benefits and their characteristic physical behaviors under different temperature, moisture, and pH conditions so that they may be included in foods that ordinarily do not contain them. One such research area is the extrusion texturization of whey proteins, which have resulted in dairy proteins with new characteristics imparted by a controlled texturization process, depending on the application desired (Hale et al., 2002 Manoi and Rizvi, 2008 Onwulata, 2009 Onwulata et al., 1998). Protein texturization is a two-step process that involves, first, the unfolding of the globular structure (denaturation) and, second, the alignments of the partially unfolded structures in the direction of mass flow in the extruder. The surface characteristics are imparted at the extruder die as the molten mass exits (Onwulata et al., 2003a). 

It also should offer promise for cell extractions, which, after all, are lipid/protein encapsulated mixtures of polar and nonpolar compounds. It would be interesting to see the effect of DMSO or DMF on the extraction of proteins. My guess is that protein might denature in 50% DMSO and precipitate so they could be filtered off or might renature and refold on lOx dilution in water and stay in solution. This might make an interesting research problem for recovering membrane-bound proteins. 

Denaturation was early observed to be a reversible process. Indeed, Anson (1 ) observed 35 years ago that hemoglobin could be heat denatured in a variety of ways and could be converted back to a state which had all the characteristics of its original native state, as determined by methods available at that time. Almost all studies of protein denaturation now revolve around not only the denaturation itself, but also its renaturation perhaps renaturation is a more interesting and provocative field for modern research. 

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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