메뉴 건너뛰기




Volumn 293, Issue 4, 1999, Pages 807-814

Turns in transmembrane helices: Determination of the minimal length of a 'Helical hairpin' and derivation of a fine-grained turn propensity scale

Author keywords

Glycosylation; Membrane protein; Protein structure; Transmembrane helix; Turn propensities

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN;

EID: 0033527670     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3183     Document Type: Article
Times cited : (90)

References (24)
  • 1
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen J., Feher G., Yeates T., Komiya H., Rees D. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc. Natl Acad. Sci. USA. 84:1987;6162-6166.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.1    Feher, G.2    Yeates, T.3    Komiya, H.4    Rees, D.5
  • 3
    • 0031563818 scopus 로고    scopus 로고
    • Helix packing in membrane proteins
    • Bowie J. U. Helix packing in membrane proteins. J. Mol. Biol. 272:1997;780-789.
    • (1997) J. Mol. Biol. , vol.272 , pp. 780-789
    • Bowie, J.U.1
  • 4
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G., Spencer R., Lee A., Barclay M., Rees D. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:1998;2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.2    Lee, A.3    Barclay, M.4    Rees, D.5
  • 5
    • 0028229579 scopus 로고
    • Folding pattern diversity of integral membrane proteins
    • Cowan S. W., Rosenbusch J. P. Folding pattern diversity of integral membrane proteins. Science. 264:1994;914-916.
    • (1994) Science , vol.264 , pp. 914-916
    • Cowan, S.W.1    Rosenbusch, J.P.2
  • 7
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D., Argos P. Knowledge-based protein secondary structure assignment. Proteins: Struct. Funct. Genet. 23:1995;566-579.
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 10
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 12
    • 0026729831 scopus 로고
    • Regulation of translation in eukaryotic systems
    • Kozak M. Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8:1992;197-225.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 197-225
    • Kozak, M.1
  • 13
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1
  • 14
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type-I single span membrane proteins
    • Landolt-Marticorena C., Williams K. A., Deber C. M., Reithmeier R. A. F. Non-random distribution of amino acids in the transmembrane segments of human type-I single span membrane proteins. J. Mol. Biol. 229:1993;602-608.
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.F.4
  • 15
    • 0025957563 scopus 로고
    • Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor
    • Liljeström P., Garoff H. Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor. J. Virol. 65:1991;147-154.
    • (1991) J. Virol. , vol.65 , pp. 147-154
    • Liljeström, P.1    Garoff, H.2
  • 16
    • 0033597281 scopus 로고    scopus 로고
    • A turn propensity scale for transmembrane helices
    • Monné M., Hermansson M., von Heijne G. A turn propensity scale for transmembrane helices. J. Mol. Biol. 288:1999;141-145.
    • (1999) J. Mol. Biol. , vol.288 , pp. 141-145
    • Monné, M.1    Hermansson, M.2    Von Heijne, G.3
  • 17
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson I., von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268:1993;5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.1    Von Heijne, G.2
  • 18
    • 0032509153 scopus 로고    scopus 로고
    • Breaking the camel's back: Proline-induced turns in a model transmembrane helix
    • Nilsson I., von Heijne G. Breaking the camel's back: proline-induced turns in a model transmembrane helix. J. Mol. Biol. 284:1998;1185-1189.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1185-1189
    • Nilsson, I.1    Von Heijne, G.2
  • 19
    • 0028101487 scopus 로고
    • The C-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson I., Whitley P., von Heijne G. The C-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol. 126:1994;1127-1132.
    • (1994) J. Cell Biol. , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    Von Heijne, G.3
  • 20
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Ångstrom from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J., Landau E. X-ray structure of bacteriorhodopsin at 2.5 Ångstrom from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.3    Landau, E.4
  • 22
    • 0030431744 scopus 로고    scopus 로고
    • Principles of membrane protein assembly and structure
    • von Heijne G. Principles of membrane protein assembly and structure. Prog. Biophys. Mol. Biol. 66:1996;113-139.
    • (1996) Prog. Biophys. Mol. Biol. , vol.66 , pp. 113-139
    • Von Heijne, G.1
  • 23
    • 0030983047 scopus 로고    scopus 로고
    • Architecture of helix bundle membrane proteins: An analysis of cytochrome c oxidase from bovine mitochondria
    • Wallin E., Tsukihara T., Yoshikawa S., von Heijne G., Elofsson A. Architecture of helix bundle membrane proteins: an analysis of cytochrome c oxidase from bovine mitochondria. Protein Sci. 6:1997;808-815.
    • (1997) Protein Sci. , vol.6 , pp. 808-815
    • Wallin, E.1    Tsukihara, T.2    Yoshikawa, S.3    Von Heijne, G.4    Elofsson, A.5
  • 24
    • 0021100176 scopus 로고
    • Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope
    • Wolfe P. B., Wickner W., Goodman J. M. Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258:1983;12073-12080.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12073-12080
    • Wolfe, P.B.1    Wickner, W.2    Goodman, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.