메뉴 건너뛰기




Volumn , Issue , 2013, Pages 161-184

Higher order structures of the caseins: A paradox?

Author keywords

[No Author keywords available]

Indexed keywords

FLEXIBLE DISPLAYS; FLEXIBLE STRUCTURES; PROTEINS;

EID: 84948962520     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-4714-6_5     Document Type: Chapter
Times cited : (9)

References (76)
  • 1
    • 0032923523 scopus 로고    scopus 로고
    • Effect of self-association of as1-casein and its cleavage fragments on aromatic circular dichroic spectra: Comparison with predicted models
    • Alaimo, M.H., Wickham, E.D. and Farrell, H.M., Jr. (1999a). Effect of self-association of aS1-casein and its cleavage fragments on aromatic circular dichroic spectra: comparison with predicted models. Biochim. Biophys. Acta. 1431, 395-409.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 395-409
    • Alaimo, M.H.1    Wickham, E.D.2    Farrell, H.M.3
  • 2
    • 0032898917 scopus 로고    scopus 로고
    • Conformational analysis of the hydrophobic peptide as1-casein (F 136-196)
    • Alaimo, M.H., Farrell, H.M., Jr. and Germann, M.W. (1999b). Conformational analysis of the hydrophobic peptide aS1-casein (f 136-196). Biochim. Biophys. Acta. 1431, 410-420.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 410-420
    • Alaimo, M.H.1    Farrell, H.M.2    Germann, M.W.3
  • 3
    • 0021474196 scopus 로고
    • Proline-containing b-turns in peptides and proteins: Analysis of structural data on globular proteins
    • Ananthanarayanan, V.S., Brahmachari, S.K. and Pattabiraman, N. (1984). Proline-containing b-turns in peptides and proteins: analysis of structural data on globular proteins. Arch. Biochem. Biophys. 232, 482-495.
    • (1984) Arch. Biochem. Biophys , vol.232 , pp. 482-495
    • Ananthanarayanan, V.S.1    Brahmachari, S.K.2    Pattabiraman, N.3
  • 4
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. (1973). Principles that govern the folding of protein chains. Science. 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.1
  • 5
    • 58249117728 scopus 로고    scopus 로고
    • Antimicrobial activity of two peptides caseci-din 15 and 17, found naturally in bovine colostrum
    • Birkemo, G.A., O’Sullivan, O., Ross, R.P. and Hill, C. (2009). Antimicrobial activity of two peptides caseci-din 15 and 17, found naturally in bovine colostrum. J. Appl. Microbiol. 106, 233-240.
    • (2009) J. Appl. Microbiol , vol.106 , pp. 233-240
    • Birkemo, G.A.1    O’ Sullivan, O.2    Ross, R.P.3    Hill, C.4
  • 6
    • 85025757105 scopus 로고
    • Raman spectroscopic study of casein structure
    • Byler, D.M., Farrell, H.M., Jr. and Susi, H. (1988). Raman spectroscopic study of casein structure. J. Dairy Sci. 71, 2622-2639.
    • (1988) J. Dairy Sci , vol.71 , pp. 2622-2639
    • Byler, D.M.1    Farrell, H.M.2    Susi, H.3
  • 7
    • 0032703108 scopus 로고    scopus 로고
    • As1-casein is required for the efficient transport of
    • Chanat, E., Martin, P. and Olivier-Bousquet M. (1999). aS1-Casein is required for the efficient transport of band K-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells. J. Cell Sci. 112, 3399-3412.
    • (1999) J. Cell Sci , vol.112 , pp. 3399-3412
    • Chanat, E.1    Martin, P.2    Olivier-Bousquet, M.3
  • 8
    • 0029267843 scopus 로고
    • Laser light scattering of model casein solutions: Effects of high temperature
    • Chu, B., Zhou, Z., Wu, G. and Farrell, H.M., Jr. (1995). Laser light scattering of model casein solutions: effects of high temperature. J. Coll. Interf. Sci. 170, 102-112.
    • (1995) J. Coll. Interf. Sci , vol.170 , pp. 102-112
    • Chu, B.1    Zhou, Z.2    Wu, G.3    Farrell, H.M.4
  • 9
    • 0023048287 scopus 로고
    • Turn prediction in proteins using a pattern-matching approach
    • Cohen, F.E., Abarbanel, R.M., Kuntz, I.D. and Fletterick, R.J. (1986). Turn prediction in proteins using a pattern-matching approach. Biochemistry. 25, 266-275.
    • (1986) Biochemistry , vol.25 , pp. 266-275
    • Cohen, F.E.1    Abarbanel, R.M.2    Kuntz, I.D.3    Fletterick, R.J.4
  • 10
    • 0019881980 scopus 로고
    • Secondary structure of bovine as1-and b-caseins in solution
    • Creamer, L.K., Richardson, T. and Parry, D.A.D. (1981). Secondary structure of bovine aS1-and b-caseins in solution. Arch. Biochem. Biophys. 211, 689-696.
    • (1981) Arch. Biochem. Biophys , vol.211 , pp. 689-696
    • Creamer, L.K.1    Richardson, T.2    Parry, D.3
  • 11
    • 0032246954 scopus 로고    scopus 로고
    • Changes in the secondary structure of bovine casein by ftir: Effects of calcium and temperature
    • Curley, D.M., Kumosinski, T.F., Unruh, J.J. and Farrell, H.M., Jr. (1998). Changes in the secondary structure of bovine casein by FTIR: effects of calcium and temperature. J. Dairy Sci. 81, 3154-3162.
    • (1998) J. Dairy Sci , vol.81 , pp. 3154-3162
    • Curley, D.M.1    Kumosinski, T.F.2    Unruh, J.J.3    Farrell, H.M.4
  • 12
    • 0019403245 scopus 로고
    • Effects of ultra-high-temperature pasteurization on milk proteins
    • Douglas, F.W. J., Greenberg, R., Farrell, H.M., Jr. and Edmondson, L.F. (1981). Effects of ultra-high-temperature pasteurization on milk proteins. J. Agr. Food Chem. 29, 11-15.
    • (1981) J. Agr. Food Chem , vol.29 , pp. 11-15
    • Douglas, F.1    Greenberg, R.2    Farrell, H.M.3    Edmondson, L.F.4
  • 13
    • 84976003334 scopus 로고
    • The temperature dependent dissociation of b-casein from bovine casein micelles and complexes
    • Downey, W.K. and Murphy, R.F. (1970). The temperature dependent dissociation of b-casein from bovine casein micelles and complexes. J. Dairy Res. 37, 361-372.
    • (1970) J. Dairy Res , vol.37 , pp. 361-372
    • Downey, W.K.1    Murphy, R.F.2
  • 15
    • 0000845298 scopus 로고
    • Physical equilibria: Proteins
    • 3rd edn., N. Wong, ed., Van Nostrand, Reinhold, New York
    • Farrell, H.M., Jr. (1988). Physical equilibria: proteins, in, Fundamentals of Dairy Chemistry, 3rd edn., N. Wong, ed., Van Nostrand, Reinhold, New York. pp 461-510.
    • (1988) Fundamentals of Dairy Chemistry , pp. 461-510
    • Farrell, H.M.1
  • 17
    • 0035177887 scopus 로고    scopus 로고
    • Secondary structural analysis of bovine caseins: Temperature dependence of b-casein structure as analyzed by circular dichroism and ftir spectroscopy and correlation with micelliza-tion
    • Farrell, H.M., Jr., Wickham, E.D., Unruh, J.J., Qi, P.X. and Hoagland, P.D. (2001). Secondary structural analysis of bovine caseins: temperature dependence of b-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micelliza-tion. Food Hydrocoll. 15, 341-354.
    • (2001) Food Hydrocoll , vol.15 , pp. 341-354
    • Farrell, H.M.1    Wickham, E.D.2    Unruh, J.J.3    Qi, P.X.4    Hoagland, P.D.5
  • 18
    • 0036362246 scopus 로고    scopus 로고
    • The caseins of milk as calcium binding proteins
    • Calcium Binding Protein Protocols, Vol. 1, G. J. Vogel, ed., Humana Press, Totowa, NJ
    • Farrell, H.M., Jr., Kumosinski, T.F., Malin, E.L. and Brown, E.M. (2002a). The caseins of milk as calcium binding proteins, in, Methods in Molecular Biology, Vol. 172, Calcium Binding Protein Protocols, Vol. 1, G. J. Vogel, ed., Humana Press, Totowa, NJ. pp 97-140.
    • (2002) Methods in Molecular Biology , vol.172 , pp. 97-140
    • Farrell, H.M.1    Kumosinski, T.F.2    Malin, E.L.3    Brown, E.M.4
  • 19
    • 0036516861 scopus 로고    scopus 로고
    • Molten globule structures in milk proteins: Implications for potential new structure-function relationships
    • Farrell, H.M., Jr., Qi, P.X., Brown, E.M., Cooke, P.H., Tunick, M.H., Wickham, E.D. and Unruh J.J. (2002b). Molten globule structures in milk proteins: implications for potential new structure-function relationships. J. Dairy Sci. 89, 459-471.
    • (2002) J. Dairy Sci , vol.89 , pp. 459-471
    • Farrell, H.M.1    Qi, P.X.2    Brown, E.M.3    Cooke, P.H.4    Tunick, M.H.5    Wickham, E.D.6    Unruh, J.J.7
  • 20
    • 0036637706 scopus 로고    scopus 로고
    • Secondary structural studies of bovine caseins: Structure and temperature dependence of b-casein phosphopeptide (1-25) as analyzed by circular dichroism, ftir spectroscopy, and analytical ultracentrifugation
    • Farrell, H.M., Jr., Qi, P.X., Wickham, E.D., and Unruh, J.J. (2002c). Secondary structural studies of bovine caseins: structure and temperature dependence of b-casein phosphopeptide (1-25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugation. J. Protein Chem. 21, 307-321.
    • (2002) J. Protein Chem , vol.21 , pp. 307-321
    • Farrell, H.M.1    Qi, P.X.2    Wickham, E.D.3    Unruh, J.J.4
  • 21
    • 12344297731 scopus 로고    scopus 로고
    • Higher order structures of caseins: A paradox? in
    • 3rd edn., Vol. 1, ProteinsPart A, P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic, Plenum Publishers, New York, NY
    • Farrell, H.M., Jr., Brown, E.M., Hoagland, P.D. and Malin, E.L. (2003a). Higher order structures of caseins: a paradox? in, Advanced Dairy Chemistry, 3rd edn., Vol. 1, ProteinsPart A, P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic, Plenum Publishers, New York, NY. pp 203-231.
    • (2003) Advanced Dairy Chemistry , pp. 203-231
    • Farrell, H.M.1    Brown, E.M.2    Hoagland, P.D.3    Malin, E.L.4
  • 22
    • 0042856750 scopus 로고    scopus 로고
    • Environmental influences on bovine k-casein: Reduction and conversion to fibrillar (amyloid) structures
    • Farrell, H.M., Jr., Cooke, P.H., Wickham, E.D., Piotrowski, E.D. and Hoagland, P.D. (2003b). Environmental influences on bovine K-casein: reduction and conversion to fibrillar (amyloid) structures. J. Protein Chem. 22, 259-273.
    • (2003) J. Protein Chem , vol.22 , pp. 259-273
    • Farrell, H.M.1    Cooke, P.H.2    Wickham, E.D.3    Piotrowski, E.D.4    Hoagland, P.D.5
  • 24
    • 33744998881 scopus 로고    scopus 로고
    • Casein micelle structure: What can be learned from milk synthesis and structural biology?
    • Farrell, H.M., Jr., Malin, E.L., Brown, E.M. and Qi, P.X. (2006a). Casein micelle structure: what can be learned from milk synthesis and structural biology? Curr. Op. Coll. & Interf. Sci. 11, 135-147.
    • (2006) Curr. Op. Coll. & Interf. Sci , vol.11 , pp. 135-147
    • Farrell, H.M.1    Malin, E.L.2    Brown, E.M.3    Qi, P.X.4
  • 25
    • 44349097173 scopus 로고    scopus 로고
    • New views of protein structure: Implications for potential new protein structure-function relationships
    • M.L. Fishman, P.X. Qi and L. Wicker, eds., American Chemical Society, Washington, DC
    • Farrell, H.M., Jr., Qi, P.X. and Uversky V.N. (2006b). New views of protein structure: implications for potential new protein structure-function relationships, in, Biopolymers: Molecules, Clusters, Networks, and Interactions, M.L. Fishman, P.X. Qi and L. Wicker, eds., American Chemical Society, Washington, DC. pp 1-18.
    • (2006) Biopolymers: Molecules, Clusters, Networks, and Interactions , pp. 1-18
    • Farrell, H.M.1    Qi, P.X.2    Uversky, V.N.3
  • 26
    • 36749050494 scopus 로고    scopus 로고
    • New views of protein structure: Applications to the caseins: Protein structure and functionality
    • Qi and L. Wicker, eds., American Chemical Society, Washington, DC
    • Farrell, H.M., Jr., Qi, P.X. and Uversky V.N. (2006c). New views of protein structure: applications to the caseins: protein structure and functionality, in, Advances in Biopolymers: Molecules, Clusters, Networks, and Interactions, M.L. Fishman, P.X. Qi and L. Wicker, eds., American Chemical Society, Washington, DC. pp 52-70.
    • (2006) Advances in Biopolymers: Molecules , pp. 52-70
    • Farrell, H.M.1    Qi, P.X.2    Uversky, V.N.3
  • 27
    • 65249088446 scopus 로고    scopus 로고
    • Review of the chemistry of as2-casein and the generation of a homologous molecular model to explain its properties
    • Farrell, H.M., Jr., Malin, E.L., Brown, E.M. and Mora-Gutierrez A. (2009). Review of the chemistry of aS2-casein and the generation of a homologous molecular model to explain its properties. J. Dairy Sci. 92, 1338-1353.
    • (2009) J. Dairy Sci , vol.92 , pp. 1338-1353
    • Farrell, H.M.1    Malin, E.L.2    Brown, E.M.3    Mora-Gutierrez, A.4
  • 28
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D.J. and Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
    • (1978) J. Mol. Biol , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 29
    • 0000645245 scopus 로고
    • On the isolation and conformation of bovine β-casein a1
    • Graham, E.R.B., Malcolm, G.M. and McKenzie, H.A. (1984). On the isolation and conformation of bovine β-casein A1. Int. J. Biol. Macromol. 6, 155-161.
    • (1984) Int. J. Biol. Macromol , vol.6 , pp. 155-161
    • Graham, E.1    Malcolm, G.M.2    McKenzie, H.A.3
  • 30
    • 0026552375 scopus 로고
    • Reexamination of the polymeric distributions of κ-casein isolated from bovine milk
    • Groves, M.L., Dower, H.J. and Farrell, H.M., Jr., (1992). Reexamination of the polymeric distributions of κ-casein isolated from bovine milk. J. Protein Chem. 11, 21-28.
    • (1992) J. Protein Chem , vol.11 , pp. 21-28
    • Groves, M.L.1    Dower, H.J.2    Farrell, H.M.3
  • 31
    • 54749100755 scopus 로고    scopus 로고
    • Environmental effects on disulfide bonding patterns of bovine κ-casein
    • Groves, M.L., Wickham, E.D. and Farrell, H.M., Jr., (1998). Environmental effects on disulfide bonding patterns of bovine κ-casein. J. Protein Chem. 17, 73-84.
    • (1998) J. Protein Chem , vol.17 , pp. 73-84
    • Groves, M.L.1    Wickham, E.D.2    Farrell, H.M.3
  • 32
    • 78049361927 scopus 로고    scopus 로고
    • Epigenetics in the extreme: Prions and the inheritance of environmentally acquired traits
    • Halfmann, R. and Lindquist, S. (2010). Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science 330, 629-632.
    • (2010) Science , vol.330 , pp. 629-632
    • Halfmann, R.1    Lindquist, S.2
  • 33
    • 0000611236 scopus 로고
    • Interaction between κ-casein and β-lactoglobulin: Possible mechanism
    • Haque, Z., Kristjansson, M. and Kinsella, J.E. (1987). Interaction between κ-casein and β-lactoglobulin: possible mechanism. J. Agric. Food Chem. 35, 644-649.
    • (1987) J. Agric. Food Chem , vol.35 , pp. 644-649
    • Haque, Z.1    Kristjansson, M.2    Kinsella, J.E.3
  • 34
    • 0035463092 scopus 로고    scopus 로고
    • Secondary structure of bovine as2-casein: Theoretical and experimental approaches
    • Hoagland, P.D., Unruh, J.J., Wickham, E.D. and Farrell, H.M., Jr. (2001). Secondary structure of bovine aS2-casein: theoretical and experimental approaches. J. Dairy Sci. 84, 1944-1949.
    • (2001) J. Dairy Sci , vol.84 , pp. 1944-1949
    • Hoagland, P.D.1    Unruh, J.J.2    Wickham, E.D.3    Farrell, H.M.4
  • 35
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins: Interpretation of primary and secondary structures of the alpha-s1-caseins, beta-caseins and kappa-caseins
    • Holt, C. and Sawyer, L. (1993). Caseins as rheomorphic proteins: interpretation of primary and secondary structures of the alpha-s1-caseins, beta-caseins and kappa-caseins. J. Chem. Soc. Faraday Trans. 89, 2683-2692.
    • (1993) J. Chem. Soc. Faraday Trans , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2
  • 36
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • Horne, D.S. (1998). Casein interactions: casting light on the black boxes, the structure in dairy products. Int. Dairy J. 8, 171-177.
    • (1998) Int. Dairy J , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 37
    • 33744991713 scopus 로고    scopus 로고
    • Casein micelle structure: Models and muddles
    • Horne, D.S. (2006). Casein micelle structure: models and muddles. Curr. Opi. Coll. & Inter. Sci. 11, 146-153.
    • (2006) Curr. Opi. Coll. & Inter. Sci , vol.11 , pp. 146-153
    • Horne, D.S.1
  • 38
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer, G., Garde, S., Garcia, A.E., Paulaitis, M.E. and Pratt, L.R. (1998). The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Nat. Acad. Sci. USA. 95, 1552-1555.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 39
    • 0028988053 scopus 로고
    • A 1h nmr study of the casein phosphopeptide as1-casein (59-79)
    • Huq, N.L., Cross, K.J. and Reynolds, E.C. (1995). A 1H NMR study of the casein phosphopeptide aS1-casein (59-79). Biochim. Biophys. Acta. 1247, 201-208.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 201-208
    • Huq, N.L.1    Cross, K.J.2    Reynolds, E.C.3
  • 40
    • 0031604586 scopus 로고    scopus 로고
    • The architecture of life
    • Ingber, D.E. (1998). The architecture of life. Scientific American.278(1), 48-57.
    • (1998) Scientific American , vol.278 , Issue.1 , pp. 48-57
    • Ingber, D.E.1
  • 41
    • 0025878090 scopus 로고
    • Calcium-induced associations of the caseins: Thermodynamic linkage of calcium binding to colloidal stability of casein micelles
    • Kumosinski, T.F. and Farrell, H.M., Jr. (1991). Calcium-induced associations of the caseins: thermodynamic linkage of calcium binding to colloidal stability of casein micelles. J. Protein Chem.10, 3-16.
    • (1991) J. Protein Chem , vol.10 , pp. 3-16
    • Kumosinski, T.F.1    Farrell, H.M.2
  • 42
    • 0345414929 scopus 로고
    • Solubility of proteins: Protein-salt-water interactions
    • N.S. Hettiarachchy and G.R. Ziegler, eds., Marcel Dekker, Inc., New York
    • Kumosinski, T.F. and Farrell, H.M., Jr. (1994). Solubility of proteins: protein-salt-water interactions, in, Protein Functionality in Food Systems, N.S. Hettiarachchy and G.R. Ziegler, eds., Marcel Dekker, Inc., New York, pp 39-77.
    • (1994) Protein Functionality in Food Systems , pp. 39-77
    • Kumosinski, T.F.1    Farrell, H.M.2
  • 43
    • 0023733240 scopus 로고
    • Determination of the quaternary structural states of bovine casein by small-angle x-ray scattering: Submicellar and micellar forms
    • Kumosinski, T.F., Pessen, H., Farrell, H.M., Jr. and Brumberger, H. (1988). Determination of the quaternary structural states of bovine casein by small-angle X-ray scattering: submicellar and micellar forms. Arch. Biochem. Biophys.266, 548-561.
    • (1988) Arch. Biochem. Biophys , vol.266 , pp. 548-561
    • Kumosinski, T.F.1    Pessen, H.2    Farrell, H.M.3    Brumberger, H.4
  • 44
    • 0027586726 scopus 로고
    • Three dimensional molecular modeling of bovine caseins: An energy-minimized b-casein structure
    • Kumosinski, T.F., Brown, E.M. and Farrell, H.M., Jr. (1993a) Three dimensional molecular modeling of bovine caseins: an energy-minimized b-casein structure. J. Dairy Sci.,76, 931-945.
    • (1993) J. Dairy Sci , vol.76 , pp. 931-945
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell, H.M.3
  • 45
    • 0027661562 scopus 로고
    • Three dimensional molecular modeling of bovine caseins: An energy minimized k-casein structure
    • Kumosinski, T.F., Brown, E.M. and Farrell, H.M., Jr. (1993b). Three dimensional molecular modeling of bovine caseins: an energy minimized K-casein structure. J. Dairy Sci.76, 2507-2520.
    • (1993) J. Dairy Sci , vol.76 , pp. 2507-2520
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell, H.M.3
  • 46
    • 0008821273 scopus 로고
    • Predicted energy minimized as1-casein working model
    • T.F. Kumosinski and M.N. Liebman, eds., ACS Symposium Series, American Chemical Society, Washington, DC
    • Kumosinski, T.F., Brown, E.M. and Farrell, H.M., Jr. (1994a). Predicted energy minimized aS1-casein working model, in, Molecular Modeling from Virtual Tools to Real Problems, T.F. Kumosinski and M.N. Liebman, eds., ACS Symposium Series 576. American Chemical Society, Washington, DC. pp 368-390.
    • (1994) Molecular Modeling from Virtual Tools to Real Problems , vol.576 , pp. 368-390
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell, H.M.3
  • 47
    • 0028567283 scopus 로고
    • An energy minimized casein submicelle working model
    • Kumosinski, T.F., King, G. and Farrell, H.M., Jr. (1994b). An energy minimized casein submicelle working model. J. Protein Chem.13, 681-700.
    • (1994) J. Protein Chem , vol.13 , pp. 681-700
    • Kumosinski, T.F.1    King, G.2    Farrell, H.M.3
  • 48
    • 0028670567 scopus 로고
    • Comparison of the three dimensional molecular models of bovine submicellar caseins with small-angle x-ray scattering. Influence of protein hydration
    • Kumosinski, T.F., King, G. and Farrell, H.M., Jr. (1994c). Comparison of the three dimensional molecular models of bovine submicellar caseins with small-angle X-ray scattering. Influence of protein hydration. J. Protein Chem.13, 701-714.
    • (1994) J. Protein Chem , vol.13 , pp. 701-714
    • Kumosinski, T.F.1    King, G.2    Farrell, H.M.3
  • 49
    • 0030524955 scopus 로고    scopus 로고
    • Correlation of refined models for casein submicelles with electron microscopic studies of casein
    • Kumosinski, T.F., Uknalis, J.J., Cooke, P.H. and Farrell, H.M., Jr. (1996). Correlation of refined models for casein submicelles with electron microscopic studies of casein. Lebens. Wiss. Technol.29, 326-333.
    • (1996) Lebens. Wiss. Technol , vol.29 , pp. 326-333
    • Kumosinski, T.F.1    Uknalis, J.J.2    Cooke, P.H.3    Farrell, H.M.4
  • 50
    • 77955369054 scopus 로고    scopus 로고
    • As1-casein, which is necessary for efficient er-golgi casein transport, is also present in a tightly membrane associated form
    • Le Parc, A., Leonil, J. and Chanat, E. (2010). aS1-Casein, which is necessary for efficient ER-Golgi casein transport, is also present in a tightly membrane associated form. BMC Cell Biology 11, 65.
    • (2010) BMC Cell Biology , vol.11 , pp. 65
    • Le Parc, A.1    Leonil, J.2    Chanat, E.3
  • 51
    • 22944433840 scopus 로고    scopus 로고
    • Contributions of terminal peptides to the associative behavior of as 1-casein
    • Malin, E.L., Brown, E.M., Wickham, E.D. and Farrell, H.M., Jr. (2005). Contributions of terminal peptides to the associative behavior of aS 1-casein. J. Dairy Sci. 88, 2318-2328.
    • (2005) J. Dairy Sci , vol.88 , pp. 2318-2328
    • Malin, E.L.1    Brown, E.M.2    Wickham, E.D.3    Farrell, H.M.4
  • 53
    • 0033405829 scopus 로고    scopus 로고
    • Casein related amyloid, characterization of a new and unique amyloid protein isolated from bovine corpora amylacea
    • Niewold, T.A., Murphy, C.L., Hulskamp-Koch, C.A., Tooten, P.C. and Gruys, E. (1999). Casein related amyloid, characterization of a new and unique amyloid protein isolated from bovine corpora amylacea. Amyloid: Int. J. Exp. Clin. Invest.6, 244-249.
    • (1999) Amyloid: Int. J. Exp. Clin. Invest , vol.6 , pp. 244-249
    • Niewold, T.A.1    Murphy, C.L.2    Hulskamp-Koch, C.A.3    Tooten, P.C.4    Gruys, E.5
  • 54
    • 0034581317 scopus 로고    scopus 로고
    • The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios
    • Onuchic, J.N., Nymeyer, A.E., Garcia, A.E., Chahine, J. and Socci, N.D. (2000). The energy landscape theory of protein folding: insights into folding mechanisms and scenarios. Adv. Protein Chem. 53, 87-152.
    • (2000) Adv. Protein Chem , vol.53 , pp. 87-152
    • Onuchic, J.N.1    Nymeyer, A.E.2    Garcia, A.E.3    Chahine, J.4    Socci, N.D.5
  • 55
    • 77949511076 scopus 로고    scopus 로고
    • Bovine chymosin: A computational study of recognition and binding of bovine k-casein
    • Palmer, D.S., Christensen, A.U., Sorensen, J., Celik, L., Qvist, K.B. and Schiott, B. (2010) Bovine chymosin: a computational study of recognition and binding of bovine K-casein. Biochemistry. 49, 2563-2573.
    • (2010) Biochemistry , vol.49 , pp. 2563-2573
    • Palmer, D.S.1    Christensen, A.U.2    Sorensen, J.3    Celik, L.4    Qvist, K.B.5    Schiott, B.6
  • 56
    • 0345436424 scopus 로고
    • Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry
    • Paulsson, M. and Dejmek, P. (1990). Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. J. Dairy Sci. 73, 590-600.
    • (1990) J. Dairy Sci , vol.73 , pp. 590-600
    • Paulsson, M.1    Dejmek, P.2
  • 57
    • 0015531025 scopus 로고
    • Casein interactions as studied by gel chromatography and ultracentrifugation
    • Pepper, L. (1972). Casein interactions as studied by gel chromatography and ultracentrifugation. Biochim. Biophys. Acta.278, 147-154.
    • (1972) Biochim. Biophys. Acta , vol.278 , pp. 147-154
    • Pepper, L.1
  • 58
    • 0006722380 scopus 로고
    • Interactions leading to the formation of casein submicelles
    • Pepper, L. and Farrell, H.M., Jr. (1982). Interactions leading to the formation of casein submicelles. J. Dairy Sci. 65, 2259-2266.
    • (1982) J. Dairy Sci , vol.65 , pp. 2259-2266
    • Pepper, L.1    Farrell, H.M.2
  • 59
    • 28644437632 scopus 로고    scopus 로고
    • Implication of c-terminal deletion on the structure and stability of bovine b-casein
    • Qi, P.X., Wickham, E.D., Piotrowski, E.G., Faegerquist, C.K., and Farrell, H.M., Jr. (2005). Implication of C-terminal deletion on the structure and stability of bovine b-casein. Protein J. 24, 431-444.
    • (2005) Protein J , vol.24 , pp. 431-444
    • Qi, P.X.1    Wickham, E.D.2    Piotrowski, E.G.3    Faegerquist, C.K.4    Farrell, H.M.5
  • 60
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • P.F. Fox, Applied Science Publishers Ltd., London
    • Schmidt, D.G. (1982). Association of caseins and casein micelle structure, in, Developments in Dairy Chemistry, P.F. Fox, ed., Applied Science Publishers Ltd., London, pp 61-86.
    • (1982) Developments in Dairy Chemistry , pp. 61-86
    • Schmidt, D.G.1
  • 61
    • 0000799754 scopus 로고
    • Micellar aspects of casein
    • E. Matijevic, ed., John Wiley and Sons, New York
    • Schmidt, D.G. and Payens, T.A.J. (1976). Micellar aspects of casein, in, Surface and Colloid Science, Vol. 9, E. Matijevic, ed., John Wiley and Sons, New York, pp 165-229.
    • (1976) Surface and Colloid Science , vol.9 , pp. 165-229
    • Schmidt, D.G.1    Payens, T.2
  • 62
    • 0015902350 scopus 로고
    • A model for the formation and structure of casein micelles from subunits of variable composition
    • Slattery, C.W. and Evard, R. (1973). A model for the formation and structure of casein micelles from subunits of variable composition. Biochim. Biophys. Acta. 317, 529-538.
    • (1973) Biochim. Biophys. Acta , vol.317 , pp. 529-538
    • Slattery, C.W.1    Evard, R.2
  • 64
    • 33749651695 scopus 로고    scopus 로고
    • Reconstituted micelle formation using reduced, carboxymethylated bovine k-casein and human b-casein
    • Sood, S.M., Lekic, T., Jhawar, H., Farrell, H.M., Jr. and Slattery, C.W. (2006). Reconstituted micelle formation using reduced, carboxymethylated bovine K-casein and human b-casein. Protein J 25, 352-360.
    • (2006) Protein J , vol.25 , pp. 352-360
    • Sood, S.M.1    Lekic, T.2    Jhawar, H.3    Farrell, H.M.4    Slattery, C.W.5
  • 65
    • 0028095571 scopus 로고
    • Crystal structure of p22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. and Reinemer, P. (1994). Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265, 383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 66
    • 0001662870 scopus 로고
    • Chemistry of milk proteins
    • P.F. Fox, ed., Applied Science Publishers, London
    • Swaisgood, H.E. (1982) Chemistry of milk proteins, in, Developments in Dairy Chemistry, Vol. 1, P.F. Fox, ed., Applied Science Publishers, London, pp 1-60.
    • (1982) Developments in Dairy Chemistry , vol.1 , pp. 1-60
    • Swaisgood, H.E.1
  • 67
    • 0036157963 scopus 로고    scopus 로고
    • A raman optical activity study of rheomorphism in caseins, synu-cleins and tau. New insights into the structure and behavior of natively unfolded proteins
    • Syme, C.D., Blanch, E.W., Holt, C., Jakes, R., Goedert, M., Hecht, L. and Barron, L.D. (2002). A Raman optical activity study of rheomorphism in caseins, synu-cleins and tau. New insights into the structure and behavior of natively unfolded proteins. Eur. J. Biochem. 269, 148-156.
    • (2002) Eur. J. Biochem , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.D.7
  • 69
    • 41149181268 scopus 로고    scopus 로고
    • Amyloid fibril formation by bovine milk as2-casein occurs under physiological conditions yet is prevented by its natural counterpart as1-casein
    • Thorn, D.C., Ecroyd, H., Sunde, M., Poon, S. and Carver, J.A. (2008). Amyloid fibril formation by bovine milk aS2-casein occurs under physiological conditions yet is prevented by its natural counterpart aS1-casein. Biochemistry 47, 3926-3936.
    • (2008) Biochemistry , vol.47 , pp. 3926-3936
    • Thorn, D.C.1    Ecroyd, H.2    Sunde, M.3    Poon, S.4    Carver, J.A.5
  • 70
    • 0023439448 scopus 로고
    • Structure of casein micelles ii. As1-casein
    • Thurn, A., Buchard, W. and Niki, R. (1987). Structure of casein micelles II. aS1-casein. Coll. Polym. Sci. 265, 897-902.
    • (1987) Coll. Polym. Sci , vol.265 , pp. 897-902
    • Thurn, A.1    Buchard, W.2    Niki, R.3
  • 71
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002). Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 72
    • 77957751076 scopus 로고    scopus 로고
    • Power law distribution defines structural disorder as a structural element directly linked with function
    • Tompa, P. and Kalmar L. (2010). Power law distribution defines structural disorder as a structural element directly linked with function. J. Mol. Biol. 403, 346-350.
    • (2010) J. Mol. Biol , vol.403 , pp. 346-350
    • Tompa, P.1    Kalmar, L.2
  • 73
    • 0030915558 scopus 로고    scopus 로고
    • Reorganization of casein submicelles in mozzarella cheese during storage
    • Tunick, M.H., Cooke, P.H., Malin E.L., Smith, P.W. and Holsinger, V.H. (1997). Reorganization of casein submicelles in Mozzarella cheese during storage. Int. Dairy J. 7, 149-155.
    • (1997) Int. Dairy J , vol.7 , pp. 149-155
    • Tunick, M.H.1    Cooke, P.H.2    Malin, E.L.3    Smith, P.W.4    Holsinger, V.H.5
  • 74
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V.N. (2002). Natively unfolded proteins: a point where biology waits for physics. Protein Science 11, 739-756.
    • (2002) Protein Science , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 75
    • 0002409037 scopus 로고
    • Formation and structure of casein micelles, in
    • H.A. McKenzie, ed., Academic Press, New York, London
    • Waugh, D.F. (1970). Formation and structure of casein micelles, in, Milk Proteins Chemistry and Molecular BiologyVol. 2, H.A. McKenzie, ed., Academic Press, New York, London, pp 3-85.
    • (1970) Milk Proteins Chemistry and Molecular Biology , vol.2 , pp. 3-85
    • Waugh, D.F.1
  • 76
    • 0026330844 scopus 로고
    • Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-a-lactalbumin
    • Xie, D., Bhakuni, V. and Freire, E. (1991). Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-a-lactalbumin. Biochemistry. 30, 10673-10678.
    • (1991) Biochemistry , vol.30 , pp. 10673-10678
    • Xie, D.1    Bhakuni, V.2    Freire, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.