H M Farrell
Affiliation: Agricultural Research Service
- Nomenclature of the proteins of cows' milk--sixth revisionH M Farrell
US Department of Agriculture, Eastern Regional Research Center, Wyndmoor, PA 19038, USA
J Dairy Sci 87:1641-74. 2004....
- Secondary structure of bovine alphaS2-casein: theoretical and experimental approachesP D Hoagland
U S Department of Agriculture, Agriculture Research Service, Eastern Regional Research Center, Wyndmoor, PA 19038, USA
J Dairy Sci 84:1944-9. 2001..As was found for other caseins studied by these spectroscopic methods, a high degree of extended beta-sheet (approximately 30%) and turns (25 to 30%) are predicted for alphaS2-casein...
- Secondary structural studies of bovine caseins: structure and temperature dependence of beta-casein phosphopeptide (1-25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugationH M Farrell
Eastern Regional Research Center Agricultural Research Service, USDA, Wyndmoor, PA 19038, USA
J Protein Chem 21:307-21. 2002..In contrast the native peptide in MD remained relatively rigid. The physical properties of the peptide suggest how phosphorylation can alter its biochemical and physiological properties...
- Solution structures of casein peptides: NMR, FTIR, CD, and molecular modeling studies of alphas1-casein, 1-23E L Malin
Eastern Regional Research Center, ARS, USDA, Wyndmoor, Pennsylvania 19038, USA
J Protein Chem 20:391-404. 2001..This information is interpreted in accord with recent spectroscopic evidence regarding the nature of unordered conformations, leading to a possible role of alphas1-casein (1-23) in facilitating casein-casein interactions...
- Contributions of terminal peptides to the associative behavior of alphas1-caseinE L Malin
US Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, Wyndmoor, PA 19038, USA
J Dairy Sci 88:2318-28. 2005..The temperature dependency of these conformational changes suggests a possible function for alphas1-casein in facilitating casein-casein interactions in casein micelle formation...
- Influence of neutral salts on the hydrothermal stability of acid-soluble collagenE M Brown
Eastern Regional Research Center, United States Department of Agriculture, Agricultural Research Service, Wyndmoor, Pennsylvania 19038, USA
J Protein Chem 19:85-92. 2000..Neutral salts, NaCl or KCl, at low concentrations (0.02-0.2 M) appear to bind to the collagens and shift the thermal transitions of these collagens to lower temperatures...
- Functionality of extrusion--texturized whey proteinsC I Onwulata
USDA, ARS, Eastern Regional Research Center, 600 E Mermaid Lane, Wyndmoor, PA 19038, USA
J Dairy Sci 86:3775-82. 2003..Varying extrusion cook temperature allowed a new controlled rate of denaturation, indicating that a texturized ingredient with a predetermined functionality based on degree of denaturation can be created...
- Review of the chemistry of alphaS2-casein and the generation of a homologous molecular model to explain its propertiesH M Farrell
Dairy Processing and Products Research Unit, USDA, Agricultural Research Service, Eastern Regional Research Center, 600 East Mermaid Lane, Wyndmoor, PA 19038, USA
J Dairy Sci 92:1338-53. 2009..In addition, most of the physiologically active peptides isolated from alpha(S2)-CN occur in this region. This structure should be viewed as a working model that can be changed as more precise experimental data are obtained...
- Molten globule structures in milk proteins: implications for potential new structure-function relationshipsH M Farrell
U S Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, Wyndmoor, PA 19038, USA
J Dairy Sci 85:459-71. 2002..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...
- Pyrroline-5-carboxylate reductase in lactating bovine mammary glandsJ J Basch
ARS, USDA, Eastern Regional Research Center, Wyndmoor, PA 19038, USA
J Dairy Sci 79:1361-8. 1996....