Submitted to: American Chemical Society Abstracts
Publication Type: Book / Chapter
Publication Acceptance Date: 10/12/2005
Publication Date: 2/25/2006
Citation: Qi, P.X., Farrell, H.M., Uversky, V.N. 2006. New view of protein structure:implications for potential new structure-function relationships:Protein Structure and Functionality American Chemical Society Symposium Book Series.p.1-18.
Technical Abstract: Recent advances in the field of protein chemistry have significantly enhanced our understanding of the possible intermediates which may occur during protein folding and unfolding. In particular, studies on alpha-lactalbumin have led to the theory that the molten globule state may be one possible intermediate in the folding of many proteins. The molten globule state is characterized by: a somewhat compact structure, a higher degree of hydration and side chain flexibility, a significant amount of native secondary structure but little tertiary folds, and the ability to react with chaperones. Other terms have been suggested for the state of proteins intermediate between the classical concepts of total random coil and compact global proteins; these are pre-molten globule, natively unfolded and intrinsically unstructured. Purified caseins are not truly random coils, but share many of the properties of these newly described intermediate states. The caseins appear to have defined secondary structures and to proceed to quaternary structures without tertiary folds. By taking advantage of this “new view” of protein folding, and applying these concepts to engineered macromolecules and food proteins, it may be possible to generate new and useful forms of proteins for the food ingredient, pharmaceutical and nanotechnology markets.