New Views of Protein Structure: Applications to the Caseins: Protein Structure and Functionality
Peptides and Proteins, Protein Structure
Digital Object Identifier (DOI)
Advances in the field of protein chemistry have enhanced our understanding of the possible intermediates which may occur during protein folding and unfolding. An enormous amount of information has been generated on folding pathways of globular proteins leading to the discovery of the molten globule state as a specific folding intermediate. Other partially folded conformations including pre-molten globule have been found that are intermediate between the random coils and compact globular conformations. Furthermore, many proteins appear as natively unfolded, intrinsically unstructured, or intrinsically disordered under physiological conditions. Purified caseins are not truly random coils, but appear to share many of the properties of these newly described intermediate states. Since casein structure is still being debated, clarifying how the caseins fit with these newly described protein states how the caseins fit with these newly described protein states would be beneficial. In this review quantitative measures based upon known physical and chemical properties of the caseins are used for their classification. By taking advantage of this "new view" of protein folding, and applying these concepts to casein fractions it may be possible to generate new potential food products from casein or casein fractions. Such products could also have neutraceutical or nanotechnological applications.
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Citation / Publisher Attribution
New Views of Protein Structure: Applications to the Caseins: Protein Structure and Functionality, in M. L. Fishman, P. X. Qi & L. Wicker (Eds.), Advances in Biopolymers, American Chemical Society, p. 52-70
Scholar Commons Citation
Farrell, Harold M. Jr.; Qi, Phoebe X.; and Uversky, Vladimir N., "New Views of Protein Structure: Applications to the Caseins: Protein Structure and Functionality" (2006). Molecular Medicine Faculty Publications. 1090.