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Volumn 34, Issue 3, 2008, Pages 309-325

Interaction between a twelve-residue segment of antifreeze protein type I, or its mutants, and water molecules

Author keywords

Angular distribution function; Antifreeze protein type I; Segments; Serine mutant; Valine mutant

Indexed keywords

AMINO ACIDS; BINDING SITES; DYNAMICS; HYDROGEN; HYDROGEN BONDS; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; PROTEINS; QUANTUM CHEMISTRY;

EID: 45849101724     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927020701830219     Document Type: Article
Times cited : (6)

References (26)
  • 1
    • 0036722371 scopus 로고    scopus 로고
    • Novel methods for rapid freezing and thawing of foods - a review
    • B. Li and D.-W. Sun, Novel methods for rapid freezing and thawing of foods - a review, J. Food Eng. 54 (2001), p. 175.
    • (2001) J. Food Eng , vol.54 , pp. 175
    • Li, B.1    Sun, D.-W.2
  • 2
    • 0002128812 scopus 로고    scopus 로고
    • Antifreeze proteins and their genes: From basic research to business opportunity
    • G.L. Fletcher, S.V. Goddard, and Y. Wu, Antifreeze proteins and their genes: From basic research to business opportunity, Chemtech 29 (1999), p. 17.
    • (1999) Chemtech , vol.29 , pp. 17
    • Fletcher, G.L.1    Goddard, S.V.2    Wu, Y.3
  • 3
    • 27844523689 scopus 로고    scopus 로고
    • Improved viability and reduced apoptosis in sub-zero 21-hour preservation of transplanted rat hearts using antifreeze proteins
    • G. Amir et al., Improved viability and reduced apoptosis in sub-zero 21-hour preservation of transplanted rat hearts using antifreeze proteins, J. Heart Lung Transplant. 24 (2005), p. 1915.
    • (2005) J. Heart Lung Transplant , vol.24 , pp. 1915
    • Amir, G.1
  • 4
    • 0024291721 scopus 로고
    • Crystal structure of an antifreeze polypeptide and its mechanistic implications
    • D.S.C. Yang et al., Crystal structure of an antifreeze polypeptide and its mechanistic implications, Nature 333 (1988), p. 232.
    • (1988) Nature , vol.333 , pp. 232
    • Yang, D.S.C.1
  • 5
    • 0025959821 scopus 로고
    • Adsorption of alphahelical antifreeze peptides on specific ice crystal surface planes
    • C.A. Knight, C.C. Cheng, and A.L. DeVries, Adsorption of alphahelical antifreeze peptides on specific ice crystal surface planes, Biophys. J. 59 (1991), p. 409.
    • (1991) Biophys. J , vol.59 , pp. 409
    • Knight, C.A.1    Cheng, C.C.2    DeVries, A.L.3
  • 6
    • 9144257407 scopus 로고    scopus 로고
    • Antifreeze proteins: Structures and mechanisms of function
    • Y. Yeh and R.E. Feeney, Antifreeze proteins: structures and mechanisms of function, Chem. Rev. 96 (1996), p. 601.
    • (1996) Chem. Rev , vol.96 , pp. 601
    • Yeh, Y.1    Feeney, R.E.2
  • 7
    • 0030817789 scopus 로고    scopus 로고
    • A diminished role for hydrogen bonds in antifreeze protein binding to ice
    • H. Chao et al., A diminished role for hydrogen bonds in antifreeze protein binding to ice, Biochemistry 36 (1997), p. 14652.
    • (1997) Biochemistry , vol.36 , pp. 14652
    • Chao, H.1
  • 8
    • 0032567416 scopus 로고    scopus 로고
    • Structure - function relationships in a type I antifreeze polypeptide
    • W. Zhang and R.A. Laursen, Structure - function relationships in a type I antifreeze polypeptide, J. Biol. Chem. 273 (1998), p. 34806.
    • (1998) J. Biol. Chem , vol.273 , pp. 34806
    • Zhang, W.1    Laursen, R.A.2
  • 9
    • 0033540633 scopus 로고    scopus 로고
    • Winter flounder 'antifreeze' proteins: Synthesis and ice growth inhibition of analogues that probe the relative importance of hydrophobic and hydrogen-bonding interactions
    • A.D.G. Haymet, L.G. Ward, and M.M. Harding, Winter flounder 'antifreeze' proteins: synthesis and ice growth inhibition of analogues that probe the relative importance of hydrophobic and hydrogen-bonding interactions, J. Am. Chem. Soc. 121 (1999), p. 941.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 941
    • Haymet, A.D.G.1    Ward, L.G.2    Harding, M.M.3
  • 10
    • 0033551242 scopus 로고    scopus 로고
    • Alternative roles for putative ice-binding residues in type I antifreeze protein
    • M.C. Loewen et al., Alternative roles for putative ice-binding residues in type I antifreeze protein, Biochemistry 38 (1999), p. 4743.
    • (1999) Biochemistry , vol.38 , pp. 4743
    • Loewen, M.C.1
  • 11
    • 2442665207 scopus 로고    scopus 로고
    • Theoretical study of interaction of winter flounder antifreeze protein with ice
    • A. Jorov, B.S. Zhorov, and D.S.C. Yang, Theoretical study of interaction of winter flounder antifreeze protein with ice, Protein Sci. 13 (2004), p. 1537.
    • (2004) Protein Sci , vol.13 , pp. 1537
    • Jorov, A.1    Zhorov, B.S.2    Yang, D.S.C.3
  • 12
    • 0030785111 scopus 로고    scopus 로고
    • Ice-binding mechanism of winter flounder antifreeze proteins
    • A. Cheng and M. Merz, Ice-binding mechanism of winter flounder antifreeze proteins, Biophys. J. 73 (1997), p. 2851.
    • (1997) Biophys. J , vol.73 , pp. 2851
    • Cheng, A.1    Merz, M.2
  • 13
    • 5444237930 scopus 로고    scopus 로고
    • Hydrogen bond analysis of type 1 antifreeze protein in water and the ice/water interface
    • P. Dalal et al., Hydrogen bond analysis of type 1 antifreeze protein in water and the ice/water interface, Phys. Chem. Commun. 4 (2001), p. 32.
    • (2001) Phys. Chem. Commun , vol.4 , pp. 32
    • Dalal, P.1
  • 14
    • 16344378406 scopus 로고    scopus 로고
    • Hydrophobic tendency of polar group hydration as a major force in type I antifreeze protein recognition
    • C. Yang and K.A. Sharp, Hydrophobic tendency of polar group hydration as a major force in type I antifreeze protein recognition, Proteins: Struct. Funct. Bioinform. 59 (2005), p. 266.
    • (2005) Proteins: Struct. Funct. Bioinform , vol.59 , pp. 266
    • Yang, C.1    Sharp, K.A.2
  • 15
    • 0032479347 scopus 로고    scopus 로고
    • Valine substituted winter flounder 'antifreeze': Preservation of ice growth hysteresis
    • A.D.G. Haymet et al., Valine substituted winter flounder 'antifreeze': Preservation of ice growth hysteresis, FEBS Lett. 430 (1998), p. 301.
    • (1998) FEBS Lett , vol.430 , pp. 301
    • Haymet, A.D.G.1
  • 17
    • 45849139572 scopus 로고    scopus 로고
    • Interaction among segments of antifreeze protein type I, or their mutants, an ice crystal and water molecules
    • submitted
    • T. Nobekawa and Y. Hagiwara, Interaction among segments of antifreeze protein type I, or their mutants, an ice crystal and water molecules, Mol. Simul., submitted.
    • Mol. Simul
    • Nobekawa, T.1    Hagiwara, Y.2
  • 19
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.J. Jorgensen et al., Comparison of simple potential functions for simulating liquid water, J. Chem. Phys. 79 (1983), p. 926.
    • (1983) J. Chem. Phys , vol.79 , pp. 926
    • Jorgensen, W.J.1
  • 20
    • 84870726202 scopus 로고    scopus 로고
    • Molecular Simulation, Academic Press, San Diego
    • D. Frenkel and B. Smit, Understanding Molecular Simulation, Academic Press, San Diego, 1996.
    • (1996) Understanding
    • Frenkel, D.1    Smit, B.2
  • 21
    • 36049060961 scopus 로고
    • Computer 'experiments' on classical fluids. II. Equilibrium correlation functions
    • L. Verlet, Computer 'experiments' on classical fluids. II. Equilibrium correlation functions, Phys. Rev. 165 (1968), p. 201.
    • (1968) Phys. Rev , vol.165 , pp. 201
    • Verlet, L.1
  • 22
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.P. Ryckart, G. Ciccotti, and H.J.C. Berendsen, Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes, J. Comput. Phys. 23 (1977), p. 327.
    • (1977) J. Comput. Phys , vol.23 , pp. 327
    • Ryckart, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 23
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins: Energy minimizations for crystals of cyclic peptides and crambin
    • W.J. Jorgensen and J. Tirado-Rives, The OPLS potential functions for proteins: Energy minimizations for crystals of cyclic peptides and crambin, J. Am. Chem. Soc. 110 (1988), p. 1657.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 1657
    • Jorgensen, W.J.1    Tirado-Rives, J.2
  • 25
    • 5444230419 scopus 로고    scopus 로고
    • Inhibition of ice nucleus growth in water by alanine dipeptide
    • K. Iwasaki and Y. Hagiwara, Inhibition of ice nucleus growth in water by alanine dipeptide, Mol. Simul. 30 (2004), p. 487.
    • (2004) Mol. Simul , vol.30 , pp. 487
    • Iwasaki, K.1    Hagiwara, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.