메뉴 건너뛰기




Volumn 4, Issue 11, 1996, Pages 1325-1337

Refined solution structure of type III antifreeze protein: Hydrophobic groups may be involved in the energetics of the protein-ice interaction

Author keywords

hydrophobic effect; ice binding affinity; NMR spectroscopy

Indexed keywords

ANIMALIA;

EID: 0030589054     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00140-2     Document Type: Article
Times cited : (167)

References (55)
  • 1
    • 0026557391 scopus 로고
    • Protein interaction with ice
    • Hew, C.L. & Yang, D.S.C. (1992). Protein interaction with ice. Eur. J. Biochem. 203, 33-42.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 33-42
    • Hew, C.L.1    Yang, D.S.C.2
  • 2
    • 0025325036 scopus 로고
    • Biochemistry of fish antifreeze proteins
    • Davies, P.L. & Hew, C.L. (1990). Biochemistry of fish antifreeze proteins. FASEB 4, 2460-2468.
    • (1990) FASEB , vol.4 , pp. 2460-2468
    • Davies, P.L.1    Hew, C.L.2
  • 3
    • 0018169486 scopus 로고
    • Antifreeze proteins from fish bloods
    • Feeney, R.E. & Yeh, Y. (1978). Antifreeze proteins from fish bloods. Adv. Protein Chem. 32, 191-282.
    • (1978) Adv. Protein Chem. , vol.32 , pp. 191-282
    • Feeney, R.E.1    Yeh, Y.2
  • 4
    • 0024291721 scopus 로고
    • Crystal structure of an antifreeze polypeptide and its mechanistic implications
    • Yang, D.S.C., Sax, M., Chakrabartty, A. & Hew, C.L. (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
  • 5
    • 0023010888 scopus 로고
    • Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus
    • Ng, N.F., Trinh, K.Y. & Hew, C.L. (1986). Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus. J. Biol. Chem. 261, 15690-15695.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15690-15695
    • Ng, N.F.1    Trinh, K.Y.2    Hew, C.L.3
  • 6
    • 0022371514 scopus 로고
    • Structure of an antifreeze polypeptide and its precursor from the ocean pout, macrozoarces americanus
    • Li, X.M., Trinh, K.Y., Hew, C.L., Buettner, B., Baenziger, J. & Davies, P.L. (1985). Structure of an antifreeze polypeptide and its precursor from the ocean pout, macrozoarces americanus. J. Biol. Chem. 260, 12904-12909.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12904-12909
    • Li, X.M.1    Trinh, K.Y.2    Hew, C.L.3    Buettner, B.4    Baenziger, J.5    Davies, P.L.6
  • 7
    • 0027536918 scopus 로고
    • The nonhelical structure of antifreeze protein type III
    • Sönnichsen, F.D., Sykes, B.D., Chao, H. & Davies, P.L. (1993). The nonhelical structure of antifreeze protein type III. Science 259, 1154-1157.
    • (1993) Science , vol.259 , pp. 1154-1157
    • Sönnichsen, F.D.1    Sykes, B.D.2    Chao, H.3    Davies, P.L.4
  • 8
    • 0026772705 scopus 로고
    • Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins
    • Ewart, K.V., Rubinsky, B. & Fletcher, G.L. (1992) Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. Biochem. Biophys. Res. Comm. 185, 335-340.
    • (1992) Biochem. Biophys. Res. Comm. , vol.185 , pp. 335-340
    • Ewart, K.V.1    Rubinsky, B.2    Fletcher, G.L.3
  • 9
    • 0027551726 scopus 로고
    • Herring antifreeze protein: Primary structure and evidence for a C-type lectin evolutionary origin
    • Ewart, K.V. & Fletcher, G.L. (1993) Herring antifreeze protein: primary structure and evidence for a C-type lectin evolutionary origin. Molecular Marine Biol. Biotech. 2, 20-27.
    • (1993) Molecular Marine Biol. Biotech. , vol.2 , pp. 20-27
    • Ewart, K.V.1    Fletcher, G.L.2
  • 10
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • Raymond, J.A. & DeVries, A.L. (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
  • 11
    • 0000555628 scopus 로고
    • Role of glycopeptides and peptides in inhibition of crystallization of water in polar fishes
    • DeVries, A.L. (1984). Role of glycopeptides and peptides in inhibition of crystallization of water in polar fishes. Phil. Trans. R. Soc. Lond. B 304, 575-588.
    • (1984) Phil. Trans. R. Soc. Lond. B , vol.304 , pp. 575-588
    • DeVries, A.L.1
  • 12
    • 0025959821 scopus 로고
    • Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes
    • Knight, C.A., Cheng, C.C. & DeVries, A.L. (1991). Adsorption of α-helical antifreeze peptides on specific ice crystal surface planes. Biophy. J. 59, 409-418.
    • (1991) Biophy. J. , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 13
    • 0027396926 scopus 로고
    • Adsorption to ice of fish antifreeze glycopeptides
    • Knight, C.A., Driggers, E. & DeVries, A.L. (1993). Adsorption to ice of fish antifreeze glycopeptides. Biophys. J. 64, 252-259.
    • (1993) Biophys. J. , vol.64 , pp. 252-259
    • Knight, C.A.1    Driggers, E.2    DeVries, A.L.3
  • 14
    • 0002037107 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish
    • diPrisco, G., ed., Springer Verlag Berlin, Heidelberg
    • Cheng, C.C. & DeVries, A.L. (1991). The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. In Life under extreme conditions. (diPrisco, G., ed.), pp. 2-14, Springer Verlag Berlin, Heidelberg.
    • (1991) Life under Extreme Conditions , pp. 2-14
    • Cheng, C.C.1    DeVries, A.L.2
  • 15
    • 0028905125 scopus 로고
    • Comparative modelling of the 3D-Structure of type II antifreeze protein
    • Sönnichsen, F.D., Sykes, B.D. & Davies, P.L. (1995). Comparative modelling of the 3D-Structure of type II antifreeze protein. Protein Sci. 4, 460-471.
    • (1995) Protein Sci. , vol.4 , pp. 460-471
    • Sönnichsen, F.D.1    Sykes, B.D.2    Davies, P.L.3
  • 16
    • 0029013417 scopus 로고
    • Ice-binding structure and mechansim of an antifreeze protein from winter flounder
    • Sicheri, F. & Yang, D.S.C. (1995). Ice-binding structure and mechansim of an antifreeze protein from winter flounder. Nature 375, 426-431.
    • (1995) Nature , vol.375 , pp. 426-431
    • Sicheri, F.1    Yang, D.S.C.2
  • 17
    • 0027946040 scopus 로고
    • Structure-function-relationship of the globular type III antifreeze protein: Identification of a cluster of hydrophilic residues required for binding to ice
    • Chao, H.L., Sönnichsen, F.D., DeLuca, C., Sykes, B.D. & Davies, P.L. (1994). Structure-function-relationship of the globular type III antifreeze protein: identification of a cluster of hydrophilic residues required for binding to ice. Protein Sci. 3, 1760-1769.
    • (1994) Protein Sci. , vol.3 , pp. 1760-1769
    • Chao, H.L.1    Sönnichsen, F.D.2    DeLuca, C.3    Sykes, B.D.4    Davies, P.L.5
  • 21
    • 0024285896 scopus 로고
    • Determination of the three-dimensional structure of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988). Determination of the three-dimensional structure of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett. 229, 317-324.
    • (1988) FEBS Lett. , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 23
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structure
    • Hyberts, S.G., Goldberg, M.S., Havel, T.F. & Wagner, G. (1992). The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structure. Protein Sci. 1, 736-751.
    • (1992) Protein Sci. , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 24
    • 0027207221 scopus 로고
    • Comparison of three algorithms for the assignment of secondary structure in proteins: The advantages of a consensus assignment
    • Culloc'h, N., Etchebest, C., Thoreau, E., Henrissat, B. & Mornon, J.-P. (1993). Comparison of three algorithms for the assignment of secondary structure in proteins: the advantages of a consensus assignment. Protein Eng. 6, 377-382.
    • (1993) Protein Eng. , vol.6 , pp. 377-382
    • Culloc'h, N.1    Etchebest, C.2    Thoreau, E.3    Henrissat, B.4    Mornon, J.-P.5
  • 26
    • 0027270959 scopus 로고
    • Use of proline mutants to solve the NMR solution structure of antifreeze protein type III
    • Chao, H.L., Sykes, B.D., Davies, P.L. & Sönnichsen, F.D. (1993). Use of proline mutants to solve the NMR solution structure of antifreeze protein type III. Protein Sci. 2, 1411-1428.
    • (1993) Protein Sci. , vol.2 , pp. 1411-1428
    • Chao, H.L.1    Sykes, B.D.2    Davies, P.L.3    Sönnichsen, F.D.4
  • 27
    • 0023656535 scopus 로고
    • Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes
    • Schrag, J.D., Cheng, C.H.C., Panico, M., Morris, H.R. & DeVries, A.L. (1987). Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes. Biochim. Biophys. Acta 915, 357-370.
    • (1987) Biochim. Biophys. Acta , vol.915 , pp. 357-370
    • Schrag, J.D.1    Cheng, C.H.C.2    Panico, M.3    Morris, H.R.4    DeVries, A.L.5
  • 28
    • 0001357768 scopus 로고
    • Antifreeze proteins from the ocean pout, macrozoarces americanus: Circular dichroism spectral studies on the native and denatured states
    • Ananthanarayanan, V.S., Slaughter, D. & Hew, C.L. (1986). Antifreeze proteins from the ocean pout, macrozoarces americanus: circular dichroism spectral studies on the native and denatured states. Biochim. Biophys. Acta 870, 154-159.
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 154-159
    • Ananthanarayanan, V.S.1    Slaughter, D.2    Hew, C.L.3
  • 29
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D. & McLachlan, A.D. (1986). Solvation energy in protein folding and binding. Science 319, 199-203.
    • (1986) Science , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 30
    • 0029861265 scopus 로고    scopus 로고
    • Effect of antifreeze protein type III dilution and mutation on the growth inhibition of ice
    • in press
    • DeLuca, C.I., Chao, H., Sönnichsen, F.D., Sykes B.D. & Davies, P.L. (1996). Effect of antifreeze protein type III dilution and mutation on the growth inhibition of ice. Biophys. J. 75(5), in press.
    • (1996) Biophys. J. , vol.75 , Issue.5
    • Deluca, C.I.1    Chao, H.2    Sönnichsen, F.D.3    Sykes, B.D.4    Davies, P.L.5
  • 31
    • 0027275364 scopus 로고
    • Structure-function relationships in an antifreeze polypeptide: The effect of added bulky groups on activity
    • Wen, D. & Laursen, R.A. (1993). Structure-function relationships in an antifreeze polypeptide: the effect of added bulky groups on activity, J. Biol. Chem. 268, 16401-16406.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16401-16406
    • Wen, D.1    Laursen, R.A.2
  • 32
    • 0028859777 scopus 로고
    • Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity
    • Chao, H., DeLuca, C.I. & Davies, P.L. (1995). Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity. FEBS Lett. 357, 183-186.
    • (1995) FEBS Lett. , vol.357 , pp. 183-186
    • Chao, H.1    DeLuca, C.I.2    Davies, P.L.3
  • 33
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. (1959). Some factors in the interpretation of protein denaturation. Adv. Protein. Chem. 14, 1-57.
    • (1959) Adv. Protein. Chem. , vol.14 , pp. 1-57
    • Kauzmann, W.1
  • 34
    • 36849117971 scopus 로고
    • Free volume and entropy in condensed systems III
    • Frank, H.S. & Evans, M.W. (1945). Free volume and entropy in condensed systems III. J. Chem. Phys. 13, 507-532.
    • (1945) J. Chem. Phys. , vol.13 , pp. 507-532
    • Frank, H.S.1    Evans, M.W.2
  • 36
    • 0028800087 scopus 로고
    • Field gradient techniques in NMR spectroscopy
    • Kay, L.E. (1995). Field gradient techniques in NMR spectroscopy. Curr. Opin. Struct. Biol. 5, 674-681.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 674-681
    • Kay, L.E.1
  • 37
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D.J., Haberkorn, R.A. & Ruben, D.J. (1982). A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Res. 48, 292-296.
    • (1982) J. Magn. Res. , vol.48 , pp. 292-296
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 38
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 39
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garret, D.S., Powers, R., Gronenborn, A.M. & Clore, G.M. (1991). A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Res. 95, 214-220.
    • (1991) J. Magn. Res. , vol.95 , pp. 214-220
    • Garret, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 40
    • 0029077856 scopus 로고
    • Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy
    • Slupski, C.M., Reinach, F.C., Smillie, L.B. & Sykes, B.D. (1995). Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy. Protein Sci. 4, 1279-1290.
    • (1995) Protein Sci. , vol.4 , pp. 1279-1290
    • Slupski, C.M.1    Reinach, F.C.2    Smillie, L.B.3    Sykes, B.D.4
  • 42
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. (1979). Investigation of exchange processes by two dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 43
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820-2820.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2820
    • Davis, D.G.1    Bax, A.2
  • 47
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of hononuclear two-dimensional NMR spectra
    • Fezik, S.W. & Zuiderweg, E.P. (1988). Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of hononuclear two-dimensional NMR spectra. J. Magn. Reson. 78, 588-593.
    • (1988) J. Magn. Reson. , vol.78 , pp. 588-593
    • Fezik, S.W.1    Zuiderweg, E.P.2
  • 49
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin C
    • Gagné, S., Tsuda, S., Li, M.X., Chandra, M., Smillie, L.B. & Sykes, B.D. (1994). Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin C. Protein Sci. 3, 1961-1974.
    • (1994) Protein Sci. , vol.3 , pp. 1961-1974
    • Gagné, S.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 50
    • 2242451043 scopus 로고
    • HMQC JFIT-software for analyzing HMQC-J spectra
    • Woodgame, M.M. & Geer, S.M. (1993). HMQC JFIT-software for analyzing HMQC-J spectra. J. Magn. Res. A 102, 246-248.
    • (1993) J. Magn. Res. A , vol.102 , pp. 246-248
    • Woodgame, M.M.1    Geer, S.M.2
  • 51
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. (1987). Ribbon models of macromolecules J. Mol. Graphics 9, 102-106.
    • (1987) J. Mol. Graphics , vol.9 , pp. 102-106
    • Carson, M.1
  • 52
    • 0021755764 scopus 로고
    • Solvent accessible surface area and excluded volume in proteins
    • Richmond, T.J. (1984). Solvent accessible surface area and excluded volume in proteins. J. Mol. Biol. 178, 63-89.
    • (1984) J. Mol. Biol. , vol.178 , pp. 63-89
    • Richmond, T.J.1
  • 53
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and Insulin
    • Shrake, A. & Rupley, J.A. (1973). Environment and exposure to solvent of protein atoms. Lysozyme and Insulin. J. Mol. Biol. 79, 351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 54
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S., Janin, J., Lesk, A.M. & Chothia, C. (1987). Interior and surface of monomeric proteins. J. Mol. Biol. 196, 641-656.
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4
  • 55
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.