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Volumn 382, Issue 3, 2008, Pages 734-746

Crystal Structure and Mutational Analysis of Ca2+-Independent Type II Antifreeze Protein from Longsnout Poacher, Brachyopsis rostratus

Author keywords

antifreeze protein; C type lectin; ice growth; thermal hysteresis; X ray structure

Indexed keywords

AMINO ACID; ANTIFREEZE PROTEIN; ISOLEUCINE; LEUCINE; PEPTIDE; PHENYLALANINE;

EID: 50149099003     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.07.042     Document Type: Article
Times cited : (63)

References (68)
  • 1
    • 0042183228 scopus 로고
    • Adsorption inhibition as a mechanism of freezing resistance in polar fishes
    • Raymond J.A., and DeVries A.L. Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc. Natl Acad. Sci. USA 74 (1977) 2589-2593
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 2589-2593
    • Raymond, J.A.1    DeVries, A.L.2
  • 2
    • 0025959821 scopus 로고
    • Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes
    • Knight C.A., Cheng C.C., and DeVries A.L. Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes. Biophys. J. 59 (1991) 409-418
    • (1991) Biophys. J. , vol.59 , pp. 409-418
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 3
    • 0022523733 scopus 로고
    • Antifreeze glycopeptides and peptides: interactions with ice and water
    • DeVries A.L. Antifreeze glycopeptides and peptides: interactions with ice and water. Methods Enzymol. 127 (1986) 293-303
    • (1986) Methods Enzymol. , vol.127 , pp. 293-303
    • DeVries, A.L.1
  • 5
    • 4344642832 scopus 로고    scopus 로고
    • Cold survival in freeze-intolerant insects
    • Graether S.P., and Sykes B.D. Cold survival in freeze-intolerant insects. Eur. J. Biochem. 271 (2004) 3285-3296
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3285-3296
    • Graether, S.P.1    Sykes, B.D.2
  • 6
    • 0034573551 scopus 로고    scopus 로고
    • Biotechnological applications of plant freezing associated proteins
    • Breton G., Danyluk J., Ouellet F., and Sarhan F. Biotechnological applications of plant freezing associated proteins. Biotechnol. Annu. Rev. 6 (2000) 59-101
    • (2000) Biotechnol. Annu. Rev. , vol.6 , pp. 59-101
    • Breton, G.1    Danyluk, J.2    Ouellet, F.3    Sarhan, F.4
  • 8
    • 1642473904 scopus 로고    scopus 로고
    • Demonstration of antifreeze protein activity in Antarctic lake bacteria
    • Gilbert J.A., Hill P.J., Dodd C.E.R., and Laybourn-Parry J. Demonstration of antifreeze protein activity in Antarctic lake bacteria. Microbiology 150 (2004) 171-180
    • (2004) Microbiology , vol.150 , pp. 171-180
    • Gilbert, J.A.1    Hill, P.J.2    Dodd, C.E.R.3    Laybourn-Parry, J.4
  • 9
    • 0034691594 scopus 로고    scopus 로고
    • Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
    • Graether S.P., Kuiper M.J., Gagne S.M., Walker V.K., Jia Z., Sykes B.D., and Davies P.L. Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 406 (2000) 325-328
    • (2000) Nature , vol.406 , pp. 325-328
    • Graether, S.P.1    Kuiper, M.J.2    Gagne, S.M.3    Walker, V.K.4    Jia, Z.5    Sykes, B.D.6    Davies, P.L.7
  • 10
    • 0002037107 scopus 로고
    • The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish
    • di Prisco G. (Ed), Springer-Verlag, Berlin
    • Cheng C.C., and DeVries A.L. The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. In: di Prisco G. (Ed). Life under Extreme Conditions (1991), Springer-Verlag, Berlin 1-14
    • (1991) Life under Extreme Conditions , pp. 1-14
    • Cheng, C.C.1    DeVries, A.L.2
  • 12
  • 13
    • 24344466982 scopus 로고    scopus 로고
    • Solution structure of an antifreeze protein CfAFP-501 from Choristoneura fumiferana
    • Li C., Guo X., Jia Z., Xia B., and Jin C. Solution structure of an antifreeze protein CfAFP-501 from Choristoneura fumiferana. J. Biomol. NMR 32 (2005) 251-256
    • (2005) J. Biomol. NMR , vol.32 , pp. 251-256
    • Li, C.1    Guo, X.2    Jia, Z.3    Xia, B.4    Jin, C.5
  • 14
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein
    • Liou Y.-C., Tocilj A., Davies P.L., and Jia Z. Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein. Nature 406 (2000) 322-324
    • (2000) Nature , vol.406 , pp. 322-324
    • Liou, Y.-C.1    Tocilj, A.2    Davies, P.L.3    Jia, Z.4
  • 15
    • 0036093824 scopus 로고    scopus 로고
    • Crystal structure of β-helical antifreeze protein points to a general ice binding model
    • Leinala E.K., Davies P.L., and Jia Z. Crystal structure of β-helical antifreeze protein points to a general ice binding model. Structure 10 (2002) 619-627
    • (2002) Structure , vol.10 , pp. 619-627
    • Leinala, E.K.1    Davies, P.L.2    Jia, Z.3
  • 16
    • 0037048649 scopus 로고    scopus 로고
    • Identification of the ice-binding face of antifreeze protein from Tenebrio molitor
    • Marshall C.B., Daley M.E., Graham L.A., Sykes B.D., and Davies P.L. Identification of the ice-binding face of antifreeze protein from Tenebrio molitor. FEBS Lett. 529 (2002) 261-267
    • (2002) FEBS Lett. , vol.529 , pp. 261-267
    • Marshall, C.B.1    Daley, M.E.2    Graham, L.A.3    Sykes, B.D.4    Davies, P.L.5
  • 17
    • 0024291721 scopus 로고
    • Crystal structure of an antifreeze polypeptide and its mechanistic implications
    • Yang D.S.C., Sax M., Chakrabartty A., and Hew C.L. Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature 333 (1988) 232-237
    • (1988) Nature , vol.333 , pp. 232-237
    • Yang, D.S.C.1    Sax, M.2    Chakrabartty, A.3    Hew, C.L.4
  • 18
    • 0025325036 scopus 로고
    • Biochemistry of fish antifreeze proteins
    • Davies P.L., and Hew C.L. Biochemistry of fish antifreeze proteins. FASEB J. 4 (1990) 2460-2468
    • (1990) FASEB J. , vol.4 , pp. 2460-2468
    • Davies, P.L.1    Hew, C.L.2
  • 21
    • 0027270959 scopus 로고
    • Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein
    • Chao H., Davies P.L., Sykes B.D., and Sönnichsen F.D. Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein. Protein Sci. 2 (1993) 1411-1428
    • (1993) Protein Sci. , vol.2 , pp. 1411-1428
    • Chao, H.1    Davies, P.L.2    Sykes, B.D.3    Sönnichsen, F.D.4
  • 22
    • 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., DeLuca C.I., Davies P.L., and Sykes B.D. Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction. Structure 4 (1996) 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
  • 23
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globular antifreeze protein to ice
    • Jia Z., DeLuca C.I., Chao H., and Davies P.L. Structural basis for the binding of a globular antifreeze protein to ice. Nature 384 (1996) 285-288
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.1    DeLuca, C.I.2    Chao, H.3    Davies, P.L.4
  • 24
    • 0032872990 scopus 로고    scopus 로고
    • Ice-binding surface of fish type III antifreeze
    • Chen G., and Jia Z. Ice-binding surface of fish type III antifreeze. Biophys. J. 77 (1999) 1602-1608
    • (1999) Biophys. J. , vol.77 , pp. 1602-1608
    • Chen, G.1    Jia, Z.2
  • 25
    • 0033597140 scopus 로고    scopus 로고
    • Quantitative and qualitative analysis of type III antifreeze protein structure and function
    • Graether S.P., DeLuca C.I., Baardsnes J., Hill G.A., Davies P.L., and Jia Z. Quantitative and qualitative analysis of type III antifreeze protein structure and function. J. Biol. Chem. 274 (1999) 11842-11847
    • (1999) J. Biol. Chem. , vol.274 , pp. 11842-11847
    • Graether, S.P.1    DeLuca, C.I.2    Baardsnes, J.3    Hill, G.A.4    Davies, P.L.5    Jia, Z.6
  • 26
    • 0031968333 scopus 로고    scopus 로고
    • Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm
    • Yang D.S., Hon W.C., Bubanko S., Xue Y., Seetharaman J., Hew C.L., and Sicheri F. Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm. Biophys. J. 74 (1998) 2142-2151
    • (1998) Biophys. J. , vol.74 , pp. 2142-2151
    • Yang, D.S.1    Hon, W.C.2    Bubanko, S.3    Xue, Y.4    Seetharaman, J.5    Hew, C.L.6    Sicheri, F.7
  • 27
    • 0032559402 scopus 로고    scopus 로고
    • The effects of steric mutations on the structure of type III antifreeze protein and its interaction with ice
    • DeLuca C.I., Davies P.L., Ye Q., and Jia Z. The effects of steric mutations on the structure of type III antifreeze protein and its interaction with ice. J. Mol. Biol. 275 (1998) 515-525
    • (1998) J. Mol. Biol. , vol.275 , pp. 515-525
    • DeLuca, C.I.1    Davies, P.L.2    Ye, Q.3    Jia, Z.4
  • 28
    • 0037137136 scopus 로고    scopus 로고
    • Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein
    • Baardsnes J., and Davies P.L. Contribution of hydrophobic residues to ice binding by fish type III antifreeze protein. Biochim. Biophys. Acta 1601 (2002) 49-54
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 49-54
    • Baardsnes, J.1    Davies, P.L.2
  • 29
    • 0026772705 scopus 로고
    • Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins
    • Ewart K.V., Rubinsky B., and Fletcher G.L. Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. Biochem. Biophys. Res. Commun. 185 (1992) 335-340
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 335-340
    • Ewart, K.V.1    Rubinsky, B.2    Fletcher, G.L.3
  • 30
    • 0026761365 scopus 로고
    • Structure of an antifreeze polypeptide from the sea raven. Disulfide bonds and similarity to lectin-binding proteins
    • Ng N.F.L., and Hew C.L. Structure of an antifreeze polypeptide from the sea raven. Disulfide bonds and similarity to lectin-binding proteins. J. Biol. Chem. 267 (1992) 16069-16075
    • (1992) J. Biol. Chem. , vol.267 , pp. 16069-16075
    • Ng, N.F.L.1    Hew, C.L.2
  • 31
    • 0027551726 scopus 로고
    • Herring antifreeze protein: primary structure and evidence for a C-type lectin evolutionary origin
    • Ewart K.V., and Fletcher G.L. Herring antifreeze protein: primary structure and evidence for a C-type lectin evolutionary origin. Mol. Mar. Biol. Chem. 2 (1993) 20-27
    • (1993) Mol. Mar. Biol. Chem. , vol.2 , pp. 20-27
    • Ewart, K.V.1    Fletcher, G.L.2
  • 32
    • 0042423587 scopus 로고    scopus 로고
    • Type II antifreeze protein from a mid-latitude freshwater fish, Japanese smelt (Hypomesus nipponensis)
    • Yamashita Y., Miura R., Takemoto Y., Tsuda S., Kawahara H., and Obata H. Type II antifreeze protein from a mid-latitude freshwater fish, Japanese smelt (Hypomesus nipponensis). Biosci. Biotechnol. Biochem. 67 (2003) 461-466
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 461-466
    • Yamashita, Y.1    Miura, R.2    Takemoto, Y.3    Tsuda, S.4    Kawahara, H.5    Obata, H.6
  • 33
    • 0001446789 scopus 로고
    • Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Clupea harengus harengus)
    • Ewart K.V., and Fletcher G.L. Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Clupea harengus harengus). Can. J. Zool. 68 (1990) 1652-1658
    • (1990) Can. J. Zool. , vol.68 , pp. 1652-1658
    • Ewart, K.V.1    Fletcher, G.L.2
  • 35
    • 0023010888 scopus 로고
    • Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus
    • Ng N.F., Trinh K.Y., and Hew C.L. Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus. J. Biol. Chem. 261 (1986) 15690-15695
    • (1986) J. Biol. Chem. , vol.261 , pp. 15690-15695
    • Ng, N.F.1    Trinh, K.Y.2    Hew, C.L.3
  • 37
    • 0032559044 scopus 로고    scopus 로고
    • The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous C-type lectin
    • Loewen M.C., Gronwald W., Sönnichsen F.D., Sykes B.D., and Davies P.L. The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous C-type lectin. Biochemistry 37 (1998) 17745-17753
    • (1998) Biochemistry , vol.37 , pp. 17745-17753
    • Loewen, M.C.1    Gronwald, W.2    Sönnichsen, F.D.3    Sykes, B.D.4    Davies, P.L.5
  • 39
    • 0030809260 scopus 로고    scopus 로고
    • wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • Perrakis A., Sixma T.K., Wilson K.S., and Lamzin V.S. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models. Acta Crystallogr., Sect. D: Biol. Crystallogr. 53 (1997) 448-455
    • (1997) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 42
  • 43
    • 0041671087 scopus 로고    scopus 로고
    • Comparative analysis of structural properties of the C-type-lectin-like domain (CTLD)
    • Zelensky A.N., and Gready J.E. Comparative analysis of structural properties of the C-type-lectin-like domain (CTLD). Proteins 52 (2003) 466-477
    • (2003) Proteins , vol.52 , pp. 466-477
    • Zelensky, A.N.1    Gready, J.E.2
  • 46
    • 0025718593 scopus 로고
    • Physical characterization and crystallization of the carbohydrate-recognition domain of a mannose-binding protein from rat
    • Weis W.I., Crichlow G.V., Murthy H.M., Hendrickson W.A., and Drickamer K. Physical characterization and crystallization of the carbohydrate-recognition domain of a mannose-binding protein from rat. J. Biol. Chem. 266 (1991) 20678-20686
    • (1991) J. Biol. Chem. , vol.266 , pp. 20678-20686
    • Weis, W.I.1    Crichlow, G.V.2    Murthy, H.M.3    Hendrickson, W.A.4    Drickamer, K.5
  • 47
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis W.I., Kahn R., Fourme R., Drickamer K., and Hendrickson W.A. Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 254 (1991) 1608-1615
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 48
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling F.T., Weis W.I., Flaherty K.M., and Brunger A.T. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271 (1996) 72-77
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brunger, A.T.4
  • 49
    • 0032558935 scopus 로고    scopus 로고
    • 2+-dependent structural changes in C-type mannose-binding proteins
    • 2+-dependent structural changes in C-type mannose-binding proteins. Biochemistry 37 (1998) 17965-17976
    • (1998) Biochemistry , vol.37 , pp. 17965-17976
    • Ng, K.K.1    Park-Snyder, S.2    Weis, W.I.3
  • 50
    • 0001044156 scopus 로고    scopus 로고
    • The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • Ewart K.V., Li Z., Yang D.S., Fletcher G.L., and Hew C.L. The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochemistry 37 (1998) 4080-4085
    • (1998) Biochemistry , vol.37 , pp. 4080-4085
    • Ewart, K.V.1    Li, Z.2    Yang, D.S.3    Fletcher, G.L.4    Hew, C.L.5
  • 51
    • 8744240300 scopus 로고    scopus 로고
    • 2+-coordinating residues of herring antifreeze protein in antifreeze activity
    • 2+-coordinating residues of herring antifreeze protein in antifreeze activity. Biochemistry 43 (2004) 14547-14554
    • (2004) Biochemistry , vol.43 , pp. 14547-14554
    • Li, Z.1    Lin, Q.2    Yang, D.S.3    Ewart, K.V.4    Hew, C.L.5
  • 52
    • 0036470053 scopus 로고    scopus 로고
    • Antifreeze proteins: an unusual receptor-ligand interaction
    • Jia Z., and Davies P.L. Antifreeze proteins: an unusual receptor-ligand interaction. Trends Biochem. Sci. 27 (2002) 101-106
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 101-106
    • Jia, Z.1    Davies, P.L.2
  • 53
    • 33746106845 scopus 로고    scopus 로고
    • Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions
    • Doxey A.C., Yaish M.W., Griffith M., and McConkey B.J. Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. Nat. Biotechnol. 24 (2006) 852-855
    • (2006) Nat. Biotechnol. , vol.24 , pp. 852-855
    • Doxey, A.C.1    Yaish, M.W.2    Griffith, M.3    McConkey, B.J.4
  • 54
    • 0028014642 scopus 로고    scopus 로고
    • Bound water molecules and conformational stabilization help mediate an antigen-antibody association
    • Bhat T.N., Bentley G.A., Boulot G., Greene M.I., Tello D., Dall'Acqua W., et al. Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Proc. Natl Acad. Sci. USA 91 (1998) 1089-1093
    • (1998) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1089-1093
    • Bhat, T.N.1    Bentley, G.A.2    Boulot, G.3    Greene, M.I.4    Tello, D.5    Dall'Acqua, W.6
  • 55
    • 0028289925 scopus 로고
    • Solvent rearrangement in an antigen-antibody interface introduced by site-directed mutagenesis of the antibody combining site
    • Ysern X., Fields B.A., Bhat T.N., Goldbaum F.A., Dall'Acqua W., Schwarz F.P., Poljak R.J., and Mariuzza R.A. Solvent rearrangement in an antigen-antibody interface introduced by site-directed mutagenesis of the antibody combining site. J. Mol. Biol. 238 (1994) 496-500
    • (1994) J. Mol. Biol. , vol.238 , pp. 496-500
    • Ysern, X.1    Fields, B.A.2    Bhat, T.N.3    Goldbaum, F.A.4    Dall'Acqua, W.5    Schwarz, F.P.6    Poljak, R.J.7    Mariuzza, R.A.8
  • 56
    • 0029856410 scopus 로고    scopus 로고
    • Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme
    • Fields B.A., Goldbaum F.A., Dall'Acqua W., Malchiodi E.L., Cauerhff A., Schwarz F.P., et al. Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme. Biochemistry 35 (1996) 15494-15503
    • (1996) Biochemistry , vol.35 , pp. 15494-15503
    • Fields, B.A.1    Goldbaum, F.A.2    Dall'Acqua, W.3    Malchiodi, E.L.4    Cauerhff, A.5    Schwarz, F.P.6
  • 57
    • 0031868554 scopus 로고    scopus 로고
    • Anatomy of an antibody molecule: structure, kinetics, thermodynamics and mutational studies of the antilysozyme antibody D1.3
    • Braden B.C., Goldman E.R., Mariuzza R.A., and Poljak R.J. Anatomy of an antibody molecule: structure, kinetics, thermodynamics and mutational studies of the antilysozyme antibody D1.3. Immunol. Rev. 163 (1998) 45-57
    • (1998) Immunol. Rev. , vol.163 , pp. 45-57
    • Braden, B.C.1    Goldman, E.R.2    Mariuzza, R.A.3    Poljak, R.J.4
  • 58
    • 0035933729 scopus 로고    scopus 로고
    • Structural evidence for entropic contribution of salt bridge formation to a protein antigen-antibody interaction: the case of hen lysozyme-HyHEL-10 Fv complex
    • Shiroishi M., Yokota A., Tsumoto K., Kondo H., Nishimiya Y., Horii K., et al. Structural evidence for entropic contribution of salt bridge formation to a protein antigen-antibody interaction: the case of hen lysozyme-HyHEL-10 Fv complex. J. Biol. Chem. 276 (2001) 23042-23050
    • (2001) J. Biol. Chem. , vol.276 , pp. 23042-23050
    • Shiroishi, M.1    Yokota, A.2    Tsumoto, K.3    Kondo, H.4    Nishimiya, Y.5    Horii, K.6
  • 59
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., and Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234 (1993) 946-950
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 62
    • 11844283348 scopus 로고    scopus 로고
    • Ice surface reconstruction as antifreeze protein-induced morphological modification mechanism
    • Strom C.S., Liu X.Y., and Jia Z. Ice surface reconstruction as antifreeze protein-induced morphological modification mechanism. J. Am. Chem. Soc. 127 (2005) 428-440
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 428-440
    • Strom, C.S.1    Liu, X.Y.2    Jia, Z.3
  • 63
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB version 2.0
    • Weeks C.M., and Miller R. The design and implementation of SnB version 2.0. J. Appl. Cryst. 32 (1999) 120-124
    • (1999) J. Appl. Cryst. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 64
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • La Fortelle E.d., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276 (1997) 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • La Fortelle, E.d.1    Bricogne, G.2
  • 65
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., and Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77 (1989) 61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 66
    • 36749050941 scopus 로고    scopus 로고
    • Effect of annealing time of an ice crystal on the activity of type III antifreeze protein
    • Takamich M., Nishimiya Y., Miura A., and Tsuda S. Effect of annealing time of an ice crystal on the activity of type III antifreeze protein. FEBS J. 274 (2007) 6469-6476
    • (2007) FEBS J. , vol.274 , pp. 6469-6476
    • Takamich, M.1    Nishimiya, Y.2    Miura, A.3    Tsuda, S.4
  • 67
    • 0029881007 scopus 로고    scopus 로고
    • Koradi, R., Billeter, M. & Wuthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 51-55, 29-32.
    • Koradi, R., Billeter, M. & Wuthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 51-55, 29-32.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.