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Volumn 15, Issue 3, 2004, Pages 437-440

Native chemical ligation of hydropobic peptides in lipid bilayer systems

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMICAL MODIFICATION; PEPTIDES; POLYPEPTIDES;

EID: 2442643066     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc049959s     Document Type: Article
Times cited : (23)

References (19)
  • 1
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
    • Kochendoerfer, G. G., Salom, D., Lear, J. D., Wilk-Orescan, R., Kent, S. B. H., and DeGrado, W. F. (1999) Total Chemical Synthesis of the Integral Membrane Protein Influenza A Virus M2: Role of Its C-Terminal Domain in Tetramer Assembly. Biochemistry 38, 11905-11913.
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.H.5    DeGrado, W.F.6
  • 2
    • 1842738226 scopus 로고    scopus 로고
    • Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis
    • Clayton, D., Shapovalov, G., Maurer, J. H., Dougherty, D. A., Lester, H. A., and Kochendoerfer, G. G. (2004) Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. 101, 4764-4769.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 4764-4769
    • Clayton, D.1    Shapovalov, G.2    Maurer, J.H.3    Dougherty, D.A.4    Lester, H.A.5    Kochendoerfer, G.G.6
  • 3
    • 1542366689 scopus 로고    scopus 로고
    • Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis
    • Kochendoerfer, G., Jones, D., Lee, S., Oblatt-Montal, M., Opella, S., and Montal, M. (2004) Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis. J. Am. Chem. Soc. 137, 2439-2446.
    • (2004) J. Am. Chem. Soc. , vol.137 , pp. 2439-2446
    • Kochendoerfer, G.1    Jones, D.2    Lee, S.3    Oblatt-Montal, M.4    Opella, S.5    Montal, M.6
  • 4
    • 0026525457 scopus 로고
    • Constructing proteins by dovetailing unprotected synthetic peptides: Backbone-engineered HIV protease
    • Schnölzer, M., and Kent, S. B. H. (1992) Constructing Proteins by Dovetailing Unprotected Synthetic Peptides: Backbone-Engineered HIV Protease. Science 256, 221-225.
    • (1992) Science , vol.256 , pp. 221-225
    • Schnölzer, M.1    Kent, S.B.H.2
  • 5
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P. E., Muir, T. W., Clark-Lewis, I., and Kent, S. B. (1994) Synthesis of proteins by native chemical ligation. Science 266, 776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 6
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson, P. E., and Kent, S. B. H. (2000) Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem 69, 923-962.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-962
    • Dawson, P.E.1    Kent, S.B.H.2
  • 7
    • 0035074833 scopus 로고    scopus 로고
    • Chemical protein synthesis methods in drug discovery
    • Kochendoerfer, G. G. (2001) Chemical protein synthesis methods in drug discovery. Curr. Opin. Drug. Discovery Dev. 4, 205-214.
    • (2001) Curr. Opin. Drug. Discovery Dev. , vol.4 , pp. 205-214
    • Kochendoerfer, G.G.1
  • 8
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir, T. W. (2003) Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249-289.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 9
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir, T. W., Sondhi, D., and Cole, P. A. (1998) Expressed protein ligation: a general method for protein engineering. Proc. Natl. Acad. Sci. U.S.A. 95, 6705-6710.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 10
    • 0033582287 scopus 로고    scopus 로고
    • Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
    • Xu, R., Ayers, B., Cowburn, D., and Muir, T. W. (1999) Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc. Natl. Acad. Sci. U.S.A. 96, 388-393.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 388-393
    • Xu, R.1    Ayers, B.2    Cowburn, D.3    Muir, T.W.4
  • 11
    • 0030482408 scopus 로고    scopus 로고
    • The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex
    • Erlanson, D. A., Chytil, M., and Verdine, G. L. (1996) The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex. Chem. Biol. 3, 981-991.
    • (1996) Chem. Biol. , vol.3 , pp. 981-991
    • Erlanson, D.A.1    Chytil, M.2    Verdine, G.L.3
  • 12
    • 0037036754 scopus 로고    scopus 로고
    • Semisynthesis and folding of the potassium channel KcsA
    • Valiyaveetil, F. I., MacKinnon, R., and Muir, T. W. (2002) Semisynthesis and folding of the potassium channel KcsA. J. Am. Chem. Soc. 124, 9113-9120.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9113-9120
    • Valiyaveetil, F.I.1    MacKinnon, R.2    Muir, T.W.3
  • 14
    • 0024603546 scopus 로고
    • Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance
    • Lindblom, G., and Rilfors, L. (1989) Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance. Biochim. Biophys. Acta 988, 221-256.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 221-256
    • Lindblom, G.1    Rilfors, L.2
  • 15
    • 0038344686 scopus 로고    scopus 로고
    • Diffusion of hydrophilic probes in bicontinuous lipidic cubic phase
    • Rowinski, P., Korytkowska, A., and Bilewicz, R. (2003) Diffusion of hydrophilic probes in bicontinuous lipidic cubic phase. Chem. Phys. Lip. 124, 147-156.
    • (2003) Chem. Phys. Lip. , vol.124 , pp. 147-156
    • Rowinski, P.1    Korytkowska, A.2    Bilewicz, R.3
  • 16
    • 0000810947 scopus 로고
    • Spectroscopic and rheological studies of enzymes in rigid lipidic matrixes: The case of α-Chymotrypsin in a lysolecithin/water cubic phase
    • Portmann, M., Landau, E. M., and Luisi, P. L. (1991) Spectroscopic and Rheological Studies of Enzymes in Rigid Lipidic Matrixes: The Case of α-Chymotrypsin in a Lysolecithin/Water cubic Phase. J. Phys. Chem. 95, 8437-8440.
    • (1991) J. Phys. Chem. , vol.95 , pp. 8437-8440
    • Portmann, M.1    Landau, E.M.2    Luisi, P.L.3
  • 18
    • 0031244525 scopus 로고    scopus 로고
    • Protein splicing and autoproteolysis mechanisms
    • Perler, F. B., Xu, M. Q., and Paulus, H. (1997) Protein splicing and autoproteolysis mechanisms. Curr. Opin. Chem. Biol. 1, 292-299.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 292-299
    • Perler, F.B.1    Xu, M.Q.2    Paulus, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.