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Volumn 73, Issue 6, 1997, Pages 2851-2873

Ice-binding mechanism of winter flounder antifreeze proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFREEZE PROTEIN; ICE;

EID: 0030785111     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78315-2     Document Type: Article
Times cited : (100)

References (46)
  • 1
    • 0024397399 scopus 로고
    • Antifreeze proteins: Structural diversity and mechanism of action
    • Ananthanarayanan, V. A. 1989. Antifreeze proteins: structural diversity and mechanism of action. Life Chem. Rep. 7:1-32.
    • (1989) Life Chem. Rep. , vol.7 , pp. 1-32
    • Ananthanarayanan, V.A.1
  • 2
    • 0027435104 scopus 로고
    • Cryogenic protection of oocytes with antifreeze proteins
    • Arav, A., B. Rubinsky, G. Fletcher, and E. Seren. 1993. Cryogenic protection of oocytes with antifreeze proteins. Mol. Reprod. Dev. 36: 488-493.
    • (1993) Mol. Reprod. Dev. , vol.36 , pp. 488-493
    • Arav, A.1    Rubinsky, B.2    Fletcher, G.3    Seren, E.4
  • 5
    • 0021763418 scopus 로고
    • Analysis of antifreeze glycoproteins in fish serum
    • Burcham, T. S., D. T. Osuga, H. Chino, and R. E. Feeney. 1984. Analysis of antifreeze glycoproteins in fish serum. Anal. Biochem. 139:197-204.
    • (1984) Anal. Biochem. , vol.139 , pp. 197-204
    • Burcham, T.S.1    Osuga, D.T.2    Chino, H.3    Feeney, R.E.4
  • 6
    • 0024962169 scopus 로고
    • Structure-function relationships in the winter flounder antifreeze polypeptide I
    • Chakrabartty, A., V. S. Ananthanarayanan, and C. L. Hew. 1989a. Structure-function relationships in the winter flounder antifreeze polypeptide I. J. Biol. Chem. 264:11307-11312.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11307-11312
    • Chakrabartty, A.1    Ananthanarayanan, V.S.2    Hew, C.L.3
  • 7
    • 0024962189 scopus 로고
    • Structure-function relationship in a winter flounder antifreeze polypeptide II
    • Chakrabartty, A., D. S. C. Yang, and C. L. Hew. 1989b. Structure-function relationship in a winter flounder antifreeze polypeptide II. J. Biol. Chem. 264:11313-11316.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11313-11316
    • Chakrabartty, A.1    Yang, D.S.C.2    Hew, C.L.3
  • 8
    • 0001207648 scopus 로고    scopus 로고
    • Application of the Nosé-Hoover chain algorithm to the study of protein dynamics
    • Cheng, A., and K. M. Merz, Jr. 1996. Application of the Nosé-Hoover chain algorithm to the study of protein dynamics. J. Phys. Chem. 100:1927-1937.
    • (1996) J. Phys. Chem. , vol.100 , pp. 1927-1937
    • Cheng, A.1    Merz K.M., Jr.2
  • 9
    • 0026599046 scopus 로고
    • Energy-optimized structure of antifreeze protein and its binding mechanism
    • Chou, K.-C. 1992. Energy-optimized structure of antifreeze protein and its binding mechanism. J. Mol. Biol. 223:509-517.
    • (1992) J. Mol. Biol. , vol.223 , pp. 509-517
    • Chou, K.-C.1
  • 11
    • 0025325036 scopus 로고
    • Biochemistry of fish antifreeze proteins
    • Davies, P. L., and C. L. Hew. 1990. Biochemistry of fish antifreeze proteins. FASEB J. 4:2460-2468.
    • (1990) FASEB J. , vol.4 , pp. 2460-2468
    • Davies, P.L.1    Hew, C.L.2
  • 12
    • 0014939615 scopus 로고
    • Chemical and physical properties of freezing point-depressing glycoproteins from antarctic fishes
    • DeVries, A. L., S. K. Komatsu, and R. E. Feeney. 1970. Chemical and physical properties of freezing point-depressing glycoproteins from antarctic fishes. J. Biol. Chem. 245:2901-2908.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2901-2908
    • DeVries, A.L.1    Komatsu, S.K.2    Feeney, R.E.3
  • 14
    • 0002428654 scopus 로고
    • Antifreeze proteins: Properties, mechanism of action, and possible applications
    • Feeney, R. E., and Y. Yeh. 1993. Antifreeze proteins: properties, mechanism of action, and possible applications. Food Technol. Jan.:82-89.
    • (1993) Food Technol. , vol.JAN. , pp. 82-89
    • Feeney, R.E.1    Yeh, Y.2
  • 15
    • 0027213263 scopus 로고
    • Calorimetric determination of inhibition of ice crystal growth by antifreeze protein in hydroxyethyl starch solutions
    • Hansen, T. N., and J. F. Carpenter. 1993. Calorimetric determination of inhibition of ice crystal growth by antifreeze protein in hydroxyethyl starch solutions. Biophys. J. 64:1843-1850.
    • (1993) Biophys. J. , vol.64 , pp. 1843-1850
    • Hansen, T.N.1    Carpenter, J.F.2
  • 16
    • 0006925174 scopus 로고
    • Interaction of antifreeze glycoproteins with liposomes
    • Abstr.
    • Hays, L. M., R. E. Feeney, L. M. Crowe, and J. H. Crowe. 1993. Interaction of antifreeze glycoproteins with liposomes. Biophys. J. 64:296a (Abstr.).
    • (1993) Biophys. J. , vol.64
    • Hays, L.M.1    Feeney, R.E.2    Crowe, L.M.3    Crowe, J.H.4
  • 17
    • 0023050471 scopus 로고
    • Biosynthesis of antifreeze polypeptides in the winter flounder characterization and seasonal occurrence of precursor polypeptides
    • Hew, C. L., C. L. Wang, S. Yan, H. Cai, A. Sclater, and G. L. Fletcher. 1986. Biosynthesis of antifreeze polypeptides in the winter flounder characterization and seasonal occurrence of precursor polypeptides. Eur. J. Biochem. 160:267-272.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 267-272
    • Hew, C.L.1    Wang, C.L.2    Yan, S.3    Cai, H.4    Sclater, A.5    Fletcher, G.L.6
  • 18
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globular antifreeze protein to ice
    • Jia, Z., C. I. DeLuca, H. Chao, and P. L. Davies. 1996. Structural basis for the binding of a globular antifreeze protein to ice. Nature. 384:285-288.
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.1    DeLuca, C.I.2    Chao, H.3    Davies, P.L.4
  • 19
    • 0027406649 scopus 로고
    • Molecular dynamics simulations of winter flounder antifreeze protein variants in solution: Correlation between side chain spacing and ice lattice
    • Jorgensen, H., H. Matsui, M. Kanaoka, H. Yanagi, Y. Yabussaki, and Y. Kikuzono. 1993. Molecular dynamics simulations of winter flounder antifreeze protein variants in solution: correlation between side chain spacing and ice lattice. Protein Engin. 6:19-27.
    • (1993) Protein Engin. , vol.6 , pp. 19-27
    • Jorgensen, H.1    Matsui, H.2    Kanaoka, M.3    Yanagi, H.4    Yabussaki, Y.5    Kikuzono, Y.6
  • 21
    • 36549101961 scopus 로고
    • The ice/water interface: A molecular dynamics simulation study
    • Karim, O. A., and A. D. J. Haymet. 1988. The ice/water interface: a molecular dynamics simulation study. J. Chem. Phys. 89:6889-6896.
    • (1988) J. Chem. Phys. , vol.89 , pp. 6889-6896
    • Karim, O.A.1    Haymet, A.D.J.2
  • 22
    • 0027674917 scopus 로고
    • Accumulation of type I fish antifreeze protein in transgenic tobacco is cold-specific
    • Kenward, K. D., M. Altschuler, D. Hildebrand, and P. L. Davies. 1993. Accumulation of type I fish antifreeze protein in transgenic tobacco is cold-specific. Plant Mol. Biol. 23:377-385.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 377-385
    • Kenward, K.D.1    Altschuler, M.2    Hildebrand, D.3    Davies, P.L.4
  • 23
    • 0343417010 scopus 로고
    • Effects of antifreeze glycoproteins on linear crystallization velocities of ice
    • Kerr, W. L., D. T. Osuga, R. E. Feeney, and Y. Yeh. 1987. Effects of antifreeze glycoproteins on linear crystallization velocities of ice. J. Cryst. Growth. 85:449-452.
    • (1987) J. Cryst. Growth. , vol.85 , pp. 449-452
    • Kerr, W.L.1    Osuga, D.T.2    Feeney, R.E.3    Yeh, Y.4
  • 24
    • 0025959821 scopus 로고
    • Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes
    • Knight, C. A., C. C. Cheng, and A. L. DeVries. 1991. Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes. Biophys. J. 59:409-418.
    • (1991) Biophys. J. , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 25
    • 0021236688 scopus 로고
    • Fish antifreeze protein and the freezing and recrystallization of ice
    • Knight, C. A., A. L. DeVries, and L. D. Oolman. 1984. Fish antifreeze protein and the freezing and recrystallization of ice. Nature. 308: 295-296.
    • (1984) Nature , vol.308 , pp. 295-296
    • Knight, C.A.1    DeVries, A.L.2    Oolman, L.D.3
  • 26
    • 0000353017 scopus 로고
    • Inhibition of ice crystal growth by preferential peptide adsorption: A molecular dynamics study
    • Lal, M., A. H. Clark, A. Lips, J. N. Ruddock, and D. N. J. White. 1993. Inhibition of ice crystal growth by preferential peptide adsorption: a molecular dynamics study. Faraday Discuss. 95:299-306.
    • (1993) Faraday Discuss. , vol.95 , pp. 299-306
    • Lal, M.1    Clark, A.H.2    Lips, A.3    Ruddock, J.N.4    White, D.N.J.5
  • 27
  • 28
    • 0027675605 scopus 로고
    • Molecular dynamics simulations of a winter flounder "antifreeze" polypeptide in aqueous solution
    • McDonald, S. M., J. W. Brady, and P. Clancy. 1993. Molecular dynamics simulations of a winter flounder "antifreeze" polypeptide in aqueous solution. Biopolymers. 33:1481-1503.
    • (1993) Biopolymers , vol.33 , pp. 1481-1503
    • McDonald, S.M.1    Brady, J.W.2    Clancy, P.3
  • 29
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilizes globular proteins
    • Myers, J. K., and C. N. Pace. 1996. Hydrogen bonding stabilizes globular proteins. Biophys. J. 71:2033-2039.
    • (1996) Biophys. J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 30
    • 0024291720 scopus 로고
    • Helices of antifreeze
    • Pain, R. H. 1988. Helices of antifreeze. Nature. 333:207-208.
    • (1988) Nature , vol.333 , pp. 207-208
    • Pain, R.H.1
  • 32
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • Raymond, J. A., and A. L. DeVries. 1977. Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc. Natl. Acad. Sci. USA. 74:2589-2593.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    DeVries, A.L.2
  • 33
    • 0018456521 scopus 로고
    • Solvation. A molecular dynamics study of a dipeptide in water
    • Rossky, P. J., and M. Karplus. 1979. Solvation. A molecular dynamics study of a dipeptide in water. J. Am. Chem. Soc. 101:1913-1937.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 1913-1937
    • Rossky, P.J.1    Karplus, M.2
  • 34
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23: 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 35
    • 0029013417 scopus 로고
    • Ice-binding structure and mechanism of an antifreeze protein from winter flounder
    • Sicheri, F., and D. S. C. Yang. 1995. Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature. 375:427-431.
    • (1995) Nature , vol.375 , pp. 427-431
    • Sicheri, F.1    Yang, D.S.C.2
  • 36
    • 0030589054 scopus 로고    scopus 로고
    • Refined solution structure of type III antifreeze protein: Hydrophobic groups may be involved in the energetics of the protein-ice interaction
    • Sönnichsen, F. D., C. I. DeLuca, P. L. Davies, and B. D. Sykes. 1996. Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction. Structure. 4:1325-1337.
    • (1996) Structure , vol.4 , pp. 1325-1337
    • Sönnichsen, F.D.1    DeLuca, C.I.2    Davies, P.L.3    Sykes, B.D.4
  • 37
    • 33947092570 scopus 로고
    • Monte Carlo studies on the structure of a dilute aqueous solution of methane
    • Swaminathan, S., S. W. Harrison, and D. L. Bereridge. 1978. Monte Carlo studies on the structure of a dilute aqueous solution of methane. J. Am. Chem. Soc. 100:5705-5712.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 5705-5712
    • Swaminathan, S.1    Harrison, S.W.2    Bereridge, D.L.3
  • 38
    • 0001554681 scopus 로고
    • Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin
    • Teeter, M. M. 1984. Water structure of a hydrophobic protein at atomic resolution: pentagon rings of water molecules in crystals of crambin. Proc. Natl. Acad. Sci. USA. 81:6014-6018.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6014-6018
    • Teeter, M.M.1
  • 39
    • 0025312879 scopus 로고
    • Molecular dynamics of protein with the OPLS potential functions. Simulation of the third domain of silver pheasant ovomucoid in water
    • Tirado-Rives, J., and W. L. Jorgensen. 1990. Molecular dynamics of protein with the OPLS potential functions. Simulation of the third domain of silver pheasant ovomucoid in water. J. Am. Chem. Soc. 112: 2773-2781.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2773-2781
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 41
    • 0027058609 scopus 로고
    • A model for binding of an antifreeze polypepetide to ice
    • Wen, D., and R. A. Laursen. 1992a. A model for binding of an antifreeze polypepetide to ice. Biophys. J. 63:1659-1662.
    • (1992) Biophys. J. , vol.63 , pp. 1659-1662
    • Wen, D.1    Laursen, R.A.2
  • 42
    • 0026623538 scopus 로고
    • Structure-function relationship in an antifreeze polypeptide
    • Wen, D., and R. A. Laursen. 1992b. Structure-function relationship in an antifreeze polypeptide. J. Biol. Chem. 267:14102-14108.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14102-14108
    • Wen, D.1    Laursen, R.A.2
  • 43
    • 0027459477 scopus 로고
    • A D-antifreeze polypeptide displays the same activity as its natural L-enantiomer
    • Wen, D., and R. A. Laursen. 1993. A D-antifreeze polypeptide displays the same activity as its natural L-enantiomer. FEBS Lett. 317:31-34.
    • (1993) FEBS Lett. , vol.317 , pp. 31-34
    • Wen, D.1    Laursen, R.A.2
  • 45
    • 0024291721 scopus 로고
    • Crystal structure of an antifreeze polypeptide and its mechanistic implications
    • Yang, D. S. C., M. Sax, A. Chakrabartty, and C. L. Hew. 1988. Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature. 333:232-237.
    • (1988) Nature , vol.333 , pp. 232-237
    • Yang, D.S.C.1    Sax, M.2    Chakrabartty, A.3    Hew, C.L.4
  • 46
    • 9144257407 scopus 로고    scopus 로고
    • Antifreeze proteins: Structures and mechanism of function
    • Yeh, Y., and R. E. Feeney. 1996. Antifreeze proteins: structures and mechanism of function. Chem. Rev. 96:601-617.
    • (1996) Chem. Rev. , vol.96 , pp. 601-617
    • Yeh, Y.1    Feeney, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.