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Volumn 100, Issue 8, 2011, Pages 2073-2074

Modeling the membrane environment for membrane proteins

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EID: 79959689910     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.02.058     Document Type: Editorial
Times cited : (16)

References (21)
  • 1
    • 77955619741 scopus 로고    scopus 로고
    • Crystallizing transmembrane peptides in lipidic mesophases
    • Höfer, N., D. Aragão, and M. Caffrey. 2010. Crystallizing transmembrane peptides in lipidic mesophases. Biophys. J. 99:L23-L25.
    • (2010) Biophys. J , vol.99
    • Höfer, N.1    Aragão, D.2    Caffrey, M.3
  • 2
    • 66049128793 scopus 로고    scopus 로고
    • Crystallizing membrane proteins for structure determination: Use of lipidic mesophases
    • Caffrey, M. 2009. Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev. Biochem. 38:29-51.
    • (2009) Annu. Rev. Biochem , vol.38 , pp. 29-51
    • Caffrey, M.1
  • 5
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs, D. A. 1988. Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science. 241:188-191.
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 6
    • 0027666089 scopus 로고
    • High-resolution structure and dynamic implications for a double-helical gramicidin A conformer
    • Pascal, S. M., and T. A. Cross. 1993. High-resolution structure and dynamic implications for a double-helical gramicidin A conformer. J. Biomol. NMR. 3:495-513.
    • (1993) J. Biomol. NMR , vol.3 , pp. 495-513
    • Pascal, S.M.1    Cross, T.A.2
  • 7
    • 0023880293 scopus 로고
    • 1 H NMR study in solution
    • DOI 10.1016/S0040-4020(01)86126-3
    • 1 H NMR study in solution. Tetrahedron. 44:925-940. (Pubitemid 18051791)
    • (1988) Tetrahedron , vol.44 , Issue.3 , pp. 925-940
    • Bystrov, V.F.1    Arseniev, A.S.2
  • 8
    • 0021892874 scopus 로고
    • 1 H-NMR study of gramicidin A transmembrane ion channel. Head-to-head right-handed, single-stranded helices
    • DOI 10.1016/0014-5793(85)80702-X
    • 1 H-NMR study of gramicidin A transmembrane ion channel. Head-to-head righthanded, single-stranded helices. FEBS Lett. 186:168-174. (Pubitemid 15070299)
    • (1985) FEBS Letters , vol.186 , Issue.2 , pp. 168-174
    • Arseniev, A.S.1    Barsukov, I.L.2    Bystrov, V.F.3
  • 9
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid- state NMR
    • Ketchem, R. R., W. Hu, and T. A. Cross. 1993. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science. 261:1457-1460. (Pubitemid 23334269)
    • (1993) Science , vol.261 , Issue.5127 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 10
    • 0031574382 scopus 로고    scopus 로고
    • High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints
    • Ketchem, R. R., B. Roux, and T. A. Cross. 1997. High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints. Structure. 5:1655-1669. (Pubitemid 28051978)
    • (1997) Structure , vol.5 , Issue.12 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 11
    • 0033162860 scopus 로고    scopus 로고
    • Gramicidin channel controversy-revisited
    • discussion 611-612
    • Cross, T. A., A. Arseniev, B. A. Wallace. 1999. Gramicidin channel controversy-revisited. Nat. Struct. Biol. 6:610-611, discussion 611-612.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 610-611
    • Cross, T.A.1    Arseniev, A.2    Wallace, B.A.3
  • 13
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • DOI 10.1021/bi980809c
    • Yau, W.-M., W. C. Wimley, S. H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37:14713-14718. (Pubitemid 28487579)
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 14
    • 23044510444 scopus 로고    scopus 로고
    • Transmembrane helices before, during, and after insertion
    • DOI 10.1016/j.sbi.2005.07.004, PII S0959440X05001260, Membranes/Engineering and Desing
    • White, S. H., and G. von Heijne. 2005. Transmembrane helices before, during, and after insertion. Curr. Opin. Struct. Biol. 15:378-386. (Pubitemid 41073827)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 378-386
    • White, S.H.1    Von Heijne, G.2
  • 15
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • DOI 10.1016/S0968-0004(00)01626-1, PII S0968000400016261
    • Killian, J. A., and G. von Heijne. 2000. How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25:429-434. (Pubitemid 30662410)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.9 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 16
    • 0023815974 scopus 로고
    • Conformation and orientation of gramicidin A in oriented phospholipid bilayers measured by solid state carbon-13 NMR
    • Cornell, B. A., F. Separovic, R. Smith. 1988. Conformation and orientation of gramicidin A in oriented phospholipid bilayers measured by solid state carbon-13 NMR. Biophys. J. 53:67-76. (Pubitemid 18009693)
    • (1988) Biophysical Journal , vol.53 , Issue.1 , pp. 67-76
    • Cornell, B.A.1    Separovic, F.2    Baldassi, A.J.3    Smith, R.4
  • 17
    • 0028100894 scopus 로고
    • Sodium ion binding in the gramicidin A channel. Solid-state NMR studies of the tryptophan residues
    • Separovic, F., J. Gehrmann, R. Smith. 1994. Sodium ion binding in the gramicidin A channel. Solid-state NMR studies of the tryptophan residues. Biophys. J. 67:1495-1500. (Pubitemid 24304322)
    • (1994) Biophysical Journal , vol.67 , Issue.4 , pp. 1495-1500
    • Separovic, F.1    Gehrmann, J.2    Milne, T.3    Cornell, B.A.4    Lin, S.Y.5    Smith, R.6
  • 18
    • 0030748570 scopus 로고    scopus 로고
    • Protein stability and conformational rearrangements in lipid bilayers: Linear gramicidin, a model system
    • Cotten, M., F. Xu, and T. A. Cross. 1997. Protein stability and conformational rearrangements in lipid bilayers: linear gramicidin, a model system. Biophys. J. 73:614-623. (Pubitemid 27337599)
    • (1997) Biophysical Journal , vol.73 , Issue.2 , pp. 614-623
    • Cotten, M.1    Xu, F.2    Cross, T.A.3
  • 20
    • 0023733886 scopus 로고
    • The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes
    • Killian, J. A., K. U. Prasad, D. W. Urry. 1988. The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes. Biochemistry. 27:4848-4855.
    • (1988) Biochemistry , vol.27 , pp. 4848-4855
    • Killian, J.A.1    Prasad, K.U.2    Urry, D.W.3
  • 21
    • 0033019673 scopus 로고    scopus 로고
    • Solid-state NMR and hydrogen-deuterium exchange in a bilayer-solubilized peptide: Structural and mechanistic implications
    • Cotten, M., R. Fu, and T. A. Cross. 1999. Solid-state NMR and hydrogen-deuterium exchange in a bilayer-solubilized peptide: structural and mechanistic implications. Biophys. J. 76:1179-1189. (Pubitemid 29262601)
    • (1999) Biophysical Journal , vol.76 , Issue.3 , pp. 1179-1189
    • Cotten, M.1    Fu, R.2    Cross, T.A.3


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