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Volumn 9, Issue 5-6, 1996, Pages 488-493

Structural Characterization and 5′-mononucleotide Binding of Polyalanine β-sheet Complexes

Author keywords

5 mononucleotide binding; Polyalanine sheet complexes; Structural characterization

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; FLUORESCENT DYE; NUCLEOTIDE; OLIGOPEPTIDE; PEPTIDE; PHOSPHODIESTERASE; POLYALANINE;

EID: 0030225349     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(199634/12)9:5/6<488::AID-JMR289>3.0.CO;2-F     Document Type: Article
Times cited : (11)

References (28)
  • 1
    • 0001763754 scopus 로고
    • Conformation-controlled hydrolysis of polyribonucleotides by sequential basic polypeptides
    • Barbier B. and Brack, A. (1995). Conformation-controlled hydrolysis of polyribonucleotides by sequential basic polypeptides. J. Am. Chem. Soc. 114, 3511-3515.
    • (1995) J. Am. Chem. Soc. , vol.114 , pp. 3511-3515
    • Barbier, B.1    Brack, A.2
  • 2
    • 0028501007 scopus 로고
    • Gene transfer with synthetic cationic amphiphiles: Prospects for gene therapy
    • Behr, J. P. (1994). Gene transfer with synthetic cationic amphiphiles: prospects for gene therapy. Bioconj. Chem. 5, 382-389.
    • (1994) Bioconj. Chem. , vol.5 , pp. 382-389
    • Behr, J.P.1
  • 4
    • 0003751509 scopus 로고
    • Hydrophobic interactions and water structure
    • ed. by A. C. Bartlett, P. C. Vapnek and L. W. McCombs, Freeman, San Francisco
    • Cantor, C. R. and Schimmel, P. R. (1980). Hydrophobic interactions and water structure. In Biophysical Chemistry Part I: The Conformation of Biological Macromolecules, ed. by A. C. Bartlett, P. C. Vapnek and L. W. McCombs, pp. 279-288. Freeman, San Francisco.
    • (1980) Biophysical Chemistry Part I: The Conformation of Biological Macromolecules , pp. 279-288
    • Cantor, C.R.1    Schimmel, P.R.2
  • 5
    • 0015906876 scopus 로고
    • The synthesis of a decapeptide with glycosidase activity
    • Chakravarty, P. K., Mathur, K. B. and Dhar, M. M. (1973). The synthesis of a decapeptide with glycosidase activity. Experientia 29, 786-788.
    • (1973) Experientia , vol.29 , pp. 786-788
    • Chakravarty, P.K.1    Mathur, K.B.2    Dhar, M.M.3
  • 6
    • 0001128585 scopus 로고
    • Convergent functional groups. 13. High-affinity complexation of adenosine derivatives within induced binding pockets
    • Conn, M. M., Deslongchamps, G., Mendoza, J. and Rebek, J. J. (1995). Convergent functional groups. 13. High-affinity complexation of adenosine derivatives within induced binding pockets. J. Am. Chem. Soc. 115, 3548-3557.
    • (1995) J. Am. Chem. Soc. , vol.115 , pp. 3548-3557
    • Conn, M.M.1    Deslongchamps, G.2    Mendoza, J.3    Rebek, J.J.4
  • 7
    • 0028105513 scopus 로고
    • Molecular recognition of nucleotides, nucleosides, and sugars by aminocyclodextrins
    • Eliseev, A. V. and Schneider, H. J. (1995). Molecular recognition of nucleotides, nucleosides, and sugars by aminocyclodextrins. J. Am. Chem. Soc. 116, 6081-6088.
    • (1995) J. Am. Chem. Soc. , vol.116 , pp. 6081-6088
    • Eliseev, A.V.1    Schneider, H.J.2
  • 9
    • 0027655718 scopus 로고
    • Polyamidoamine cascade polymers mediate efficient transfection of cells in culture
    • Haensler, J. and Szoka, F. C. J. (1993). Polyamidoamine cascade polymers mediate efficient transfection of cells in culture. Bioconj. Chem. 4, 372-379.
    • (1993) Bioconj. Chem. , vol.4 , pp. 372-379
    • Haensler, J.1    Szoka, F.C.J.2
  • 10
    • 0025335121 scopus 로고
    • Design and synthesis of a peptide having chymotrypsin-like esterase activity
    • Hahn, K. W., Klis, W. A. and Stewart, J. M. (1990). Design and synthesis of a peptide having chymotrypsin-like esterase activity. Science 248, 1544-1547.
    • (1990) Science , vol.248 , pp. 1544-1547
    • Hahn, K.W.1    Klis, W.A.2    Stewart, J.M.3
  • 11
    • 0027177971 scopus 로고
    • Metal ion-dependent modulation of the dynamics of a designed protein
    • Handel, T. M., Williams, S. A. and DeGrado, W. F. (1993a). Metal ion-dependent modulation of the dynamics of a designed protein. Science 261, 879-885.
    • (1993) Science , vol.261 , pp. 879-885
    • Handel, T.M.1    Williams, S.A.2    DeGrado, W.F.3
  • 13
    • 0000478940 scopus 로고
    • General method for the rapid solid-phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual amino acids
    • Houghten, R. A. (1985). General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids. Proc. Natl. Acad. Sci. USA 482, 5131-5135.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.482 , pp. 5131-5135
    • Houghten, R.A.1
  • 14
    • 0022728936 scopus 로고
    • Simplified procedure for carrying out simultaneous multiple hydrogen fluoride cleavages of protected peptide resins
    • Houghten, R. A., Bray, M. K., De Graw, S. T. and Kirby, C. J. (1986). Simplified procedure for carrying out simultaneous multiple hydrogen fluoride cleavages of protected peptide resins. Int. J. Protein Res. 27, 673-678.
    • (1986) Int. J. Protein Res. , vol.27 , pp. 673-678
    • Houghten, R.A.1    Bray, M.K.2    De Graw, S.T.3    Kirby, C.J.4
  • 15
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C. Jr (1990). Protein secondary structure and circular dichroism: a practical guide. Proteins: Struct. Func. Genet. 7, 205-214.
    • (1990) Proteins: Struct. Func. Genet. , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 18
    • 0018084369 scopus 로고
    • 5′-Nucleotide pohsphodiesterase: Isolation of covalently bound 5′-adenosine monophosphate, an intermediate in the catalytic mechanism
    • Landt, M. and Butler, L. G. (1978). 5′-Nucleotide pohsphodiesterase: isolation of covalently bound 5′-adenosine monophosphate, an intermediate in the catalytic mechanism. Biochemistry 17, 4130-4135.
    • (1978) Biochemistry , vol.17 , pp. 4130-4135
    • Landt, M.1    Butler, L.G.2
  • 19
    • 0028483545 scopus 로고
    • Reactivity of organic anions promoted by a quaternary ammonium ion dendrimer
    • Lee, J. J., Ford, W. T., Moore, J. A. and Li, Y. (1994). Reactivity of organic anions promoted by a quaternary ammonium ion dendrimer. Macromolecules 27, 4632-4634.
    • (1994) Macromolecules , vol.27 , pp. 4632-4634
    • Lee, J.J.1    Ford, W.T.2    Moore, J.A.3    Li, Y.4
  • 20
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., Robbins, V. H. and Baldwin, R. L. (1989). Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. USA 86, 5286-5290.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 21
    • 0028535167 scopus 로고
    • Synthetic peptides as binding-step based catalytic mimics
    • Pérez-Payá, E., Houghten, R. A. and Blondelle, S. E. (1994). Synthetic peptides as binding-step based catalytic mimics. Pept. Res. 7, 286-288.
    • (1994) Pept. Res. , vol.7 , pp. 286-288
    • Pérez-Payá, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 23
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenymethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M. and Bolen, D. D. (1988). Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenymethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.D.2
  • 24
    • 0013800421 scopus 로고
    • The interaction of naphthalene dye with apomyoglobin and apohemoglobin
    • Stryer, L. (1965). The interaction of naphthalene dye with apomyoglobin and apohemoglobin. J. Mol. Biol. 13, 482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 25
    • 13344276445 scopus 로고
    • N2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: Evidence and application in peptide synthesis
    • N2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: evidence and application in peptide synthesis. J. Am. Chem. Soc. 105, 6442-6455.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6442-6455
    • Tam, J.P.1    Heath, W.F.2    Merrifield, R.B.3
  • 27
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • Zhang, S., Holmes, T., Lockshin, C. and Rich, A. (1993). Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc. Natl. Acad. Sci. USA 90, 3334-3338.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 28
    • 0028184678 scopus 로고
    • Unusually stable β-sheet formation in an ionic self-complementary oligopeptide
    • Zhang, S., Lockshin, C., Cook, R. and Rich, A. (1994). Unusually stable β-sheet formation in an ionic self-complementary oligopeptide. Biopolymers 34, 663-672.
    • (1994) Biopolymers , vol.34 , pp. 663-672
    • Zhang, S.1    Lockshin, C.2    Cook, R.3    Rich, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.