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Volumn 272, Issue 5, 1997, Pages 780-789

Helix packing in membrane proteins

Author keywords

Bacteriorhodopsin; Cytochrome c oxidase; Photosynthetic reaction center; Protein structure

Indexed keywords

MEMBRANE PROTEIN;

EID: 0031563818     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1279     Document Type: Article
Times cited : (281)

References (40)
  • 1
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams P., Arkin I., Engelman D., Brünger A. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Struct. Biol. 2:1995;154-162.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 154-162
    • Adams, P.1    Arkin, I.2    Engelman, D.3    Brünger, A.4
  • 3
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G-protein-coupled receptors
    • Baldwin J. The probable arrangement of the helices in G-protein-coupled receptors. EMBO J. 12:1993;1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.1
  • 4
    • 0029768644 scopus 로고    scopus 로고
    • Helix-helix interactions in lipid bilayers
    • Ben-Tal N., Honig B. Helix-helix interactions in lipid bilayers. Biophys. J. 71:1996;3046-3050.
    • (1996) Biophys. J. , vol.71 , pp. 3046-3050
    • Ben-Tal, N.1    Honig, B.2
  • 6
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerization and transmembrane signalling
    • Bormann B., Engelman D. Intramembrane helix-helix association in oligomerization and transmembrane signalling. Annu. Rev. Biophys. Biomol. Struct. 21:1992;233-242.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 233-242
    • Bormann, B.1    Engelman, D.2
  • 7
    • 0024557054 scopus 로고
    • Synthetic peptides mimic the assembly of transmembrane glycoproteins
    • Bormann B., Knowles W., Marchesi V. Synthetic peptides mimic the assembly of transmembrane glycoproteins. J. Biol. Chem. 264:1989;4033.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4033
    • Bormann, B.1    Knowles, W.2    Marchesi, V.3
  • 8
  • 9
    • 0025784505 scopus 로고
    • Structure of the membrane-bound protein photosynthetic reaction center fromRhodobacter sphaeroides
    • Chang C., El-Kabbani O., Tiede D., Norris J., Shiffer M. Structure of the membrane-bound protein photosynthetic reaction center fromRhodobacter sphaeroides. Biochemistry. 30:1991;5352-5369.
    • (1991) Biochemistry , vol.30 , pp. 5352-5369
    • Chang, C.1    El-Kabbani, O.2    Tiede, D.3    Norris, J.4    Shiffer, M.5
  • 11
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled coils
    • Crick F. The packing of α-helices: simple coiled coils. Acta Crystallog. 6:1953;689-697.
    • (1953) Acta Crystallog. , vol.6 , pp. 689-697
    • Crick, F.1
  • 12
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber C. M., Li S. -C. Peptides in membranes: helicity and hydrophobicity. Biopolymers. 37:1995;295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.-C.2
  • 13
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureus
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureus. Biochemistry. 20:1981;2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 14
    • 0005384356 scopus 로고
    • Nobel Lecture: The photosynthetic reaction centre from the purple bacteriumRhodopseudomonas viridus
    • Deisenhofer J., Michel H. Nobel Lecture: The photosynthetic reaction centre from the purple bacteriumRhodopseudomonas viridus. EMBO J. 8:1989;2149-2169.
    • (1989) EMBO J. , vol.8 , pp. 2149-2169
    • Deisenhofer, J.1    Michel, H.2
  • 15
    • 0027244433 scopus 로고
    • Quadradic minimization of predictors for protein secondary structure. Application to transmembrane α-helices
    • Edelman J. Quadradic minimization of predictors for protein secondary structure. Application to transmembrane α-helices. J. Mol. Biol. 232:1993;165-191.
    • (1993) J. Mol. Biol. , vol.232 , pp. 165-191
    • Edelman, J.1
  • 16
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman D., Steitz T., Goldman A. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15:1986;321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.1    Steitz, T.2    Goldman, A.3
  • 17
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff N., Ceska T., Downing K., Baldwin J., Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259:1996;393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.2    Downing, K.3    Baldwin, J.4    Henderson, R.5
  • 18
    • 0025292355 scopus 로고
    • Model of the structure of bacteriorhodopsin based on high resolution cryo-electron microscopy
    • Henderson R., Baldwin J., Ceska T., Zemlin F., Beckmann E., Downing K. Model of the structure of bacteriorhodopsin based on high resolution cryo-electron microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.2    Ceska, T.3    Zemlin, F.4    Beckmann, E.5    Downing, K.6
  • 19
    • 0024968216 scopus 로고
    • Orientation of alpha-helical peptides in a lipid bilayer
    • Huschilt J., Millman B., Davis J. Orientation of alpha-helical peptides in a lipid bilayer. Biochim. Biophys. Acta. 979:1989;139-141.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 139-141
    • Huschilt, J.1    Millman, B.2    Davis, J.3
  • 20
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochromecParacoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochromecParacoccus 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
  • 21
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones D., Taylor W., Thornton J. A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry. 33:1994;3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.1    Taylor, W.2    Thornton, J.3
  • 22
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 24
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J., Engelman D. Membrane protein folding and oligomerization: the two-stage model. Biochemistry. 29:1990;4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.1    Engelman, D.2
  • 25
    • 0027507711 scopus 로고
    • Packing of secondary structural elements in proteins. Analysis and prediction of inter-helix distances
    • Reddy B., Blundell T. Packing of secondary structural elements in proteins. Analysis and prediction of inter-helix distances. J. Mol. Biol. 233:1993;464-479.
    • (1993) J. Mol. Biol. , vol.233 , pp. 464-479
    • Reddy, B.1    Blundell, T.2
  • 26
    • 0017876485 scopus 로고
    • Packing of α-helices: Geometrical constraints and contact areas
    • Richmond T., Richards F. Packing of α-helices: geometrical constraints and contact areas. J. Mol. Biol. 119:1978;537-555.
    • (1978) J. Mol. Biol. , vol.119 , pp. 537-555
    • Richmond, T.1    Richards, F.2
  • 27
    • 0031012140 scopus 로고    scopus 로고
    • Slow α-helix formation during folding of a membrane protein
    • Riley M., Wallace B., Flitsch S., Booth P. Slow α-helix formation during folding of a membrane protein. Biochemistry. 36:1997;192-196.
    • (1997) Biochemistry , vol.36 , pp. 192-196
    • Riley, M.1    Wallace, B.2    Flitsch, S.3    Booth, P.4
  • 29
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins and 86% accuracy
    • Rost B., Fariselli P., Casadio R. Topology prediction for helical transmembrane proteins and 86% accuracy. Protein Sci. 5:1996;1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 31
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • Sipos L., von Heijne G. Predicting the topology of eukaryotic membrane proteins. Eur. J. Biochem. 213:1993;1333-1340.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1333-1340
    • Sipos, L.1    Von Heijne, G.2
  • 32
    • 0029086391 scopus 로고
    • A continuum theory for the prediction of lateral and rotational positioning of α-helices in membrane proteins: Bacteriorhodopsin
    • Suwa M., Hirokawa T., Mitaku S. A continuum theory for the prediction of lateral and rotational positioning of α-helices in membrane proteins: bacteriorhodopsin. Proteins: Struct. Funct. Genet. 22:1995;363-377.
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 363-377
    • Suwa, M.1    Hirokawa, T.2    Mitaku, S.3
  • 33
    • 0028175436 scopus 로고
    • A method for α-helical integral membrane protein fold prediction
    • Taylor W., Jones D., Green N. A method for α-helical integral membrane protein fold prediction. Proteins: Struct. Funct. Genet. 18:1994;281-294.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 281-294
    • Taylor, W.1    Jones, D.2    Green, N.3
  • 34
    • 0027092981 scopus 로고
    • The glycophorin A transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helices
    • Treutlein H., Lemmon M., Engelman D., Brunger A. The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices. Biochemistry. 31:1992;12726.
    • (1992) Biochemistry , vol.31 , pp. 12726
    • Treutlein, H.1    Lemmon, M.2    Engelman, D.3    Brunger, A.4
  • 36
    • 0028280699 scopus 로고
    • Prediction of the positioning of the seven transmembrane α-helices of bacteriorhodopsin
    • Tuffery P., Etchebest C., Popot J. -L., Lavery R. Prediction of the positioning of the seven transmembrane α-helices of bacteriorhodopsin. J. Mol. Biol. 236:1994;1105-1123.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1105-1123
    • Tuffery, P.1    Etchebest, C.2    Popot, J.-L.3    Lavery, R.4
  • 37
    • 0026716643 scopus 로고
    • Membrane protein structure prediction: Hydrophobicity analysis and the postive-inside rule
    • von Heijne G. Membrane protein structure prediction: Hydrophobicity analysis and the postive-inside rule. J. Mol. Biol. 225:1992;487.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487
    • Von Heijne, G.1
  • 39
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: The helical lattice superposition model
    • Walther D., Eisenhaber F., Argos P. Principles of helix-helix packing in proteins: the helical lattice superposition model. J. Mol. Biol. 25:1996;536-553.
    • (1996) J. Mol. Biol. , vol.25 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.