New Views of Protein Structure: Implications for Potential New Protein Structure-function Relationships
Food, Hydration, Nucleic Acid Structure, Protein Folding, Protein Structure
Digital Object Identifier (DOI)
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 α-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 compact structure, a high degree of hydration and side chain flexibility, a significant amount of native secondary structure but little tertiary structure, and the ability to react with chaperones. Other partially folded conformations (e.g., pre-molten globule) have also been found. Many proteins known as natively unfolded, intrinsically unstructured, or intrinsically disordered were shown to be highly flexible under physiological conditions. 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 nanotechnological markets.
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Citation / Publisher Attribution
New Views of Protein Structure: Implications for Potential New Protein Structure-Function Relationships, in M. L. Fishman, P. X. Qi & L. Wicker (Eds.), Advances in Biopolymers, American Chemical Society, p. 1-18
Scholar Commons Citation
Farrell, Harold M. Jr.; Qi, Phoebe X.; and Uversky, Vladimir N., "New Views of Protein Structure: Implications for Potential New Protein Structure-function Relationships" (2006). Molecular Medicine Faculty Publications. 1034.