| Autor: |
Farrell HM Jr; U.S. Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, Wyndmoor, PA 19038, USA. hfarrell@arserrc.gov, Qi PX, Brown EM, Cooke PH, Tunick MH, Wickham ED, Unruh JJ |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of dairy science [J Dairy Sci] 2002 Mar; Vol. 85 (3), pp. 459-71. |
| DOI: |
10.3168/jds.S0022-0302(02)74096-4 |
| Abstrakt: |
Recent advances in the field of protein chemistry have significantly enhanced our understanding of the possible intermediates that 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 a 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. Purified alpha(s1)- and kappa-caseins share many of these same properties; these caseins may thus occur naturally in a molten globule-like state with defined, persistent structures. The caseins appear to have defined secondary structures and to proceed to quaternary structures without tertiary folds. This process may be explained, in part, by comparison with the architectural concepts of tensegrity. By taking advantage of this "new view" of protein folding, and applying these concepts to dairy proteins, it may be possible to generate new and useful forms of proteins for the food ingredient market. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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