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Volumn 85, Issue 3, 2002, Pages 459-471

Molten globule structures in milk proteins: Implications for potential new structure-function relationships

Author keywords

Casein structure; Protein folding; Spectroscopy of proteins; Whey proteins

Indexed keywords

CASEIN; CHAPERONE; CHELATING AGENT; GUANIDINE; LACTALBUMIN; MILK PROTEIN;

EID: 0036516861     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(02)74096-4     Document Type: Conference Paper
Times cited : (85)

References (31)
  • 1
    • 0022762429 scopus 로고
    • Radioimmunoassay for measurement of bovine α-lactalbumin in serum, milk and tissue culture media
    • Akers, R. M., T. B. McFadden, W. E. Beal, A. J. Guidry, and H. M. Farrell. 1986. Radioimmunoassay for measurement of bovine α-lactalbumin in serum, milk and tissue culture media. J. Dairy Res. 53:419-429.
    • (1986) J. Dairy Res. , vol.53 , pp. 419-429
    • Akers, R.M.1    McFadden, T.B.2    Beal, W.E.3    Guidry, A.J.4    Farrell, H.M.5
  • 3
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai, M., and K. Kuwajima. 2000. Role of the molten globule state in protein folding. Adv. Protein Chem. 53:209-282.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 4
    • 85025757105 scopus 로고
    • Raman spectroscopic study of casein structure
    • Byler, D. M., H. M., Farrell, Jr., and H. Susi. 1988. Raman spectroscopic study of casein structure. J. Dairy Sci. 71:2622-2629.
    • (1988) J. Dairy Sci. , vol.71 , pp. 2622-2629
    • Byler, D.M.1    Farrell Jr., H.M.2    Susi, H.3
  • 7
    • 12344297731 scopus 로고    scopus 로고
    • Higher order structures of caseins: A paradox
    • P. Fox and P. McSweeney, eds. (in press). Kluwer Academic, NY, NY
    • Farrell, H. M., Jr., E. M. Brown, P. D. Hoagland, and E. L. Malin. 2002a. Higher order structures of caseins: a paradox. In Advanced Dairy Chemistry. P. Fox and P. McSweeney, eds. (in press). Kluwer Academic, NY, NY.
    • (2002) Advanced Dairy Chemistry
    • Farrell Jr., H.M.1    Brown, E.M.2    Hoagland, P.D.3    Malin, E.L.4
  • 12
    • 0026552375 scopus 로고
    • Reexamination of the polymeric distribution of β-casein isolated from bovine milk
    • Groves, M. L., H. J. Dower, and H. M. Farrell, Jr. 1992. Reexamination of the polymeric distribution of β-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 Jr., H.M.3
  • 14
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins
    • Holt, C., and L. Sawyer. 1993. Caseins as rheomorphic proteins. J. Chem. Soc. Faraday 89:2683-2690.
    • (1993) J. Chem. Soc. Faraday , vol.89 , pp. 2683-2690
    • Holt, C.1    Sawyer, L.2
  • 15
    • 0031604586 scopus 로고    scopus 로고
    • The architecture of life
    • Ingber, D. E. 1998. The architecture of life. Sci. Am. Jan. pp 48-57.
    • (1998) Sci. Am. Jan. , pp. 48-57
    • Ingber, D.E.1
  • 16
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke, R., and H. Lilie. 2000. Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53:329-401.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 17
    • 0031050429 scopus 로고    scopus 로고
    • Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering
    • Kataoka, M., K. Kuwajima, F. Tokonaga, and Y. Goto. 1997. Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering. Protein Sci. 6:422-430.
    • (1997) Protein Sci. , vol.6 , pp. 422-430
    • Kataoka, M.1    Kuwajima, K.2    Tokonaga, F.3    Goto, Y.4
  • 18
    • 0020120012 scopus 로고
    • Structure and mechanism of action of riboflavin binding protein
    • Kumosinski, T. F., H. Pessen, and H. M. Farrell, Jr. 1982. Structure and mechanism of action of riboflavin binding protein. Arch. Biochem. Biophys. 214:714-725.
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 714-725
    • Kumosinski, T.F.1    Pessen, H.2    Farrell Jr., H.M.3
  • 19
    • 0027661562 scopus 로고
    • Three dimensional molecular modeling of caseins: An energy minimized κ-casein structure
    • Kumosinski, T. F., E. M. Brown, and H. M. Farrell, Jr. 1993. Three dimensional molecular modeling of caseins: an energy minimized κ-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 Jr., H.M.3
  • 20
    • 0030372755 scopus 로고    scopus 로고
    • Quantitation of the global secondary structure of globular proteins by FTIR spectroscopy
    • Kumonsinski, T. F., and J. J. Unruh. 1996. Quantitation of the global secondary structure of globular proteins by FTIR spectroscopy. Talanta 43:199-219.
    • (1996) Talanta , vol.43 , pp. 199-219
    • Kumonsinski, T.F.1    Unruh, J.J.2
  • 21
    • 0028838951 scopus 로고
    • The hydrophobic nature of Gro EL-substrate binding
    • Lin, Z., F. P. Schwarz, and E. Eisenstein. 1995. The hydrophobic nature of Gro EL-substrate binding. J. Biol. Chem. 270:1011-1014.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1011-1014
    • Lin, Z.1    Schwarz, F.P.2    Eisenstein, E.3
  • 22
    • 0642333026 scopus 로고    scopus 로고
    • Oxygen-17 NMR studies of bovine and caprine caseins: Hydration and activity in deuterated sugar solutions
    • Mora-Gutierrez, A., T. F. Kumosinski, and H. M. Farrell, Jr. 1997. Oxygen-17 NMR studies of bovine and caprine caseins: hydration and activity in deuterated sugar solutions. J. Agric. Food Chem. 12:4545-4553.
    • (1997) J. Agric. Food Chem. , vol.12 , pp. 4545-4553
    • Mora-Gutierrez, A.1    Kumosinski, T.F.2    Farrell Jr., H.M.3
  • 23
    • 0034581317 scopus 로고    scopus 로고
    • The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios
    • Onuchic, J. N., H. Nymeyer, A. E. Garcia, J. Chahine, and N. D. Socci. 2000. The energy landscape theory of protein folding: Insights into folding mechanisms and scenarios. Adv. Protein Chem. 53:88-153.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 88-153
    • Onuchic, J.N.1    Nymeyer, H.2    Garcia, A.E.3    Chahine, J.4    Socci, N.D.5
  • 24
    • 0345436424 scopus 로고
    • Thermal denaturation of whey proteins in mixtures with caseins studied by calorimetry
    • Paulsson, M., and P. Dejmek. 1990. Thermal denaturation of whey proteins in mixtures with caseins studied by calorimetry. J. Dairy Sci. 73:590-600.
    • (1990) J. Dairy Sci. , vol.73 , pp. 590-600
    • Paulsson, M.1    Dejmek, P.2
  • 25
    • 0034581622 scopus 로고    scopus 로고
    • Autonomous protein folding units
    • Peng, Z.-Y., and L. C. Wu. 2000. Autonomous protein folding units. Adv. Protein Chem. 53:1-49.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 1-49
    • Peng, Z.-Y.1    Wu, L.C.2
  • 26
    • 0030585408 scopus 로고    scopus 로고
    • Crystal structures of guinea-pig, goat and bovine α-lactalbumin
    • Pike, A. C., K. Brew, and K. R. Achorya. 1996. Crystal structures of guinea-pig, goat and bovine α-lactalbumin. Structure 4:691-703.
    • (1996) Structure , vol.4 , pp. 691-703
    • Pike, A.C.1    Brew, K.2    Achorya, K.R.3
  • 27
    • 0033407049 scopus 로고    scopus 로고
    • Molecular dynamics model structures for the molten globule state of α-lactalbumin
    • Saito, M. 1999. Molecular dynamics model structures for the molten globule state of α-lactalbumin. Protein Eng. 12:1097-1104.
    • (1999) Protein Eng. , vol.12 , pp. 1097-1104
    • Saito, M.1
  • 28
    • 0033548540 scopus 로고    scopus 로고
    • Side chain conformational disorder in a molten globule
    • Smith, L. J., C. M. Dobson, and W. F. van Gunsteren. 1999. Side chain conformational disorder in a molten globule. J. Mol. Biol. 286:1567-1580.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1567-1580
    • Smith, L.J.1    Dobson, C.M.2    Van Gunsteren, W.F.3
  • 30
    • 0001662870 scopus 로고
    • Chemistry of milk proteins
    • P. F. Fox ed. Applied Science London, United Kingdom
    • Swaisgood, H. E. 1982. Chemistry of milk proteins. Pages 1-60 in Developments in Dairy Chemistry. P. F. Fox ed. Applied Science London, United Kingdom.
    • (1982) Developments in Dairy Chemistry , pp. 1-60
    • Swaisgood, H.E.1
  • 31
    • 0026330844 scopus 로고
    • Calorimetric determination of the energetics of the molten globule intermediate in protein folding
    • Xie, D., V. Bhakuni, and E. Freire. 1991. Calorimetric determination of the energetics of the molten globule intermediate in protein folding. 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.