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Åkerfeldt KS, Lear JD, Wasserman ZR, Chung LA, DeGrado WF Synthetic peptides as models for ion channel proteins. Acc Chem Res. 26:1993;191-197.
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Design of molecular function: Channels of communication
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Montal M Design of molecular function: channels of communication. Annu Rev Biophys Biomol Struct. 24:1995;31-57.
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+ conduction and selectivity
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+ ions somewhat like valinomycin.
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+ ions somewhat like valinomycin.
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Doyle, D.A.1
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Chait, B.T.7
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4
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0031902085
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Protein design - On the threshold of functional properties
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A useful overview of the TASP (template-assisted synthetic protein) approach to protein design and assembly, including some comments on applications to channel proteins. TASP methodology has the potential to define and orient transmembrane structures more precisely than can be done by relying upon the spontaneous oligomerization of short membrane-active peptides.
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Tuchscherer G, Scheibler L, Dumy P, Mutter M Protein design - on the threshold of functional properties. Biopolymers. 47:1998;63-73. A useful overview of the TASP (template-assisted synthetic protein) approach to protein design and assembly, including some comments on applications to channel proteins. TASP methodology has the potential to define and orient transmembrane structures more precisely than can be done by relying upon the spontaneous oligomerization of short membrane-active peptides.
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Biopolymers
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Tuchscherer, G.1
Scheibler, L.2
Dumy, P.3
Mutter, M.4
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5
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0027403316
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Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
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Montal MO, Iwamoto T, Tomich JM, Montal M Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor. FEBS Lett. 320:1993;261-266.
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Montal, M.O.1
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Tomich, J.M.3
Montal, M.4
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0028127099
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Template-assembled melittin: Structural and functional characterization of a designed, synthetic channel-forming protein
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Pawlak M, Meseth U, Dhanapal B, Mutter M, Vogel H Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein. Protein Sci. 3:1994;1788-1805.
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Pawlak, M.1
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Vogel, H.5
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7
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1842555216
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Ion channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by the barrel stave model
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Matsubara A, Asami K, Akagi A, Nishino N: Ion channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by the barrel stave model. J Chem Soc Chem Commun 1996, 2069-2070.
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Matsubara, A.1
Asami, K.2
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Nishino, N.4
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8
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0030851379
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Intrinsic rectification of ion flux in alamethicin channels - studies with an alamethicin dimer
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Woolley GA, Biggin PC, Schultz A, Lien L, Jaikaran DCJ, Breed J, Crowhurst K, Sansom MSP Intrinsic rectification of ion flux in alamethicin channels - studies with an alamethicin dimer. Biophys J. 73:1997;770-778.
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Woolley, G.A.1
Biggin, P.C.2
Schultz, A.3
Lien, L.4
Jaikaran, D.C.J.5
Breed, J.6
Crowhurst, K.7
Sansom, M.S.P.8
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10
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0030964855
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De novo design, synthesis, and characterization of a pore-forming small globular protein and its insertion into lipid bilayers
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A 69 amino acid four-helix bundle, in which a hydrophobic helix is surrounded by three others, was synthesized following a design loosely based on the structures of channel-forming bacterial colicins. The polypeptide, which is a globular monomer in solution, assembles into membranes to form low conductance channels. Further progress in this area will require definitive structural information on both the water-soluble and assembled forms of the protein.
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Lee S, Kiyota T, Kunitake T, Matsumoto E, Yamashita S, Anzai K, Sugihara G De novo design, synthesis, and characterization of a pore-forming small globular protein and its insertion into lipid bilayers. Biochemistry. 36:1997;3782-3791. A 69 amino acid four-helix bundle, in which a hydrophobic helix is surrounded by three others, was synthesized following a design loosely based on the structures of channel-forming bacterial colicins. The polypeptide, which is a globular monomer in solution, assembles into membranes to form low conductance channels. Further progress in this area will require definitive structural information on both the water-soluble and assembled forms of the protein.
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(1997)
Biochemistry
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Lee, S.1
Kiyota, T.2
Kunitake, T.3
Matsumoto, E.4
Yamashita, S.5
Anzai, K.6
Sugihara, G.7
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11
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0031857720
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Peptide nanotubes and beyond
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A review of recent progress on nanotubes based on cyclic peptides, which self assemble in lipid bilayers in a predictable way to form well-defined transmembrane channels. The first examples contained an even number of alternating D- and L-α-amino acids. Recently, cyclic β peptides have been used to make a new class of nanotubes.
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Hartgerink JD, Clark TD, Ghadiri MR Peptide nanotubes and beyond. Chem Eur J. 4:1998;1367-1372. A review of recent progress on nanotubes based on cyclic peptides, which self assemble in lipid bilayers in a predictable way to form well-defined transmembrane channels. The first examples contained an even number of alternating D- and L-α-amino acids. Recently, cyclic β peptides have been used to make a new class of nanotubes.
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Chem Eur J
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, pp. 1367-1372
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Hartgerink, J.D.1
Clark, T.D.2
Ghadiri, M.R.3
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13
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0346249753
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Electrical activity of artificial ion channels incorporated into planar lipid bilayers
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Voyer N, Potvin L, Rousseau E: Electrical activity of artificial ion channels incorporated into planar lipid bilayers. J Chem Soc Perkin Trans 2 1997, 1469-1471.
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J Chem Soc Perkin Trans 2
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Voyer, N.1
Potvin, L.2
Rousseau, E.3
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0030905756
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A synthetic transmembrane ion channel active in lipid bilayers
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Meillon JC, Voyer N A synthetic transmembrane ion channel active in lipid bilayers. Angew Chem Int Ed Engl. 36:1997;967-969.
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Angew Chem Int Ed Engl
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Meillon, J.C.1
Voyer, N.2
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16
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0032478974
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Importance of tryptophan dipoles for protein function - 5-fluorination of tryptophans in gramicidin A channels
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Andersen OS, Greathouse DV, Providence LL, Becker MD, Koeppe RE Importance of tryptophan dipoles for protein function - 5-fluorination of tryptophans in gramicidin A channels. J Am Chem Soc. 120:1998;5142-5146.
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Andersen, O.S.1
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Providence, L.L.3
Becker, M.D.4
Koeppe, R.E.5
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Characterization of thermal isomerization at the single molecule level
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Jaikaran DCJ, Woolley GA Characterization of thermal isomerization at the single molecule level. J Phys Chem. 99:1995;13352-13355.
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0030731890
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Voltage-dependent behavior of a ball-and-chain gramicidin channel
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Woolley GA, Zunic V, Karanicolas J, Jaikaran ASI, Starostin AV Voltage-dependent behavior of a ball-and-chain gramicidin channel. Biophys J. 73:1997;2465-2475.
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Woolley, G.A.1
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Karanicolas, J.3
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Starostin, A.V.5
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20
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0031194564
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Designed protein pores as components for biosensors
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An engineered staphylococcal α-hemolysin is described with a divalent metal cation binding site in the lumen of the transmembrane channel. By exploiting single-channel recording, the designed pore can be used as an element in a stochastic sensor, which both identifies metal ions and quantitates them. The paper also introduces technology for purifying hetero-oligomeric channels and pores.
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Braha O, Walker B, Cheley S, Kasianowicz JJ, Song L, Gouaux JE, Bayley H Designed protein pores as components for biosensors. Chem Biol. 4:1997;497-505. An engineered staphylococcal α-hemolysin is described with a divalent metal cation binding site in the lumen of the transmembrane channel. By exploiting single-channel recording, the designed pore can be used as an element in a stochastic sensor, which both identifies metal ions and quantitates them. The paper also introduces technology for purifying hetero-oligomeric channels and pores.
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(1997)
Chem Biol
, vol.4
, pp. 497-505
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Braha, O.1
Walker, B.2
Cheley, S.3
Kasianowicz, J.J.4
Song, L.5
Gouaux, J.E.6
Bayley, H.7
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21
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0031853989
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Porin mutants with new channel properties
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Mutations in a porin from Rhodopseudomonas blastica are described, which affect single channel conductance. The crystal structures of many of the new proteins are described, putting the analysis of their functional properties on far more solid ground than is usual.
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Schmid B, Maveyraud L, Kromer M, Schulz GE Porin mutants with new channel properties. Protein Sci. 7:1998;1603-1611. Mutations in a porin from Rhodopseudomonas blastica are described, which affect single channel conductance. The crystal structures of many of the new proteins are described, putting the analysis of their functional properties on far more solid ground than is usual.
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Protein Sci
, vol.7
, pp. 1603-1611
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Schmid, B.1
Maveyraud, L.2
Kromer, M.3
Schulz, G.E.4
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23
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0032503999
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Specific covalent labeling of recombinant protein molecules inside living cells
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A paper that will make us think anew about the targeted modification of proteins, including channels and pores. Methods that go beyond single-cysteine modification are needed. This paper presents one possibility, two-pronged trivalent arsenic reagents directed at tetracysteine motifs, and may stimulate renewed effort in this area.
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Griffin BA, Adams SR, Tsien RY Specific covalent labeling of recombinant protein molecules inside living cells. Science. 281:1998;269-272. A paper that will make us think anew about the targeted modification of proteins, including channels and pores. Methods that go beyond single-cysteine modification are needed. This paper presents one possibility, two-pronged trivalent arsenic reagents directed at tetracysteine motifs, and may stimulate renewed effort in this area.
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(1998)
Science
, vol.281
, pp. 269-272
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Griffin, B.A.1
Adams, S.R.2
Tsien, R.Y.3
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24
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0030895628
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Caged cysteine and thiophosphoryl peptides
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Pan P, Bayley H Caged cysteine and thiophosphoryl peptides. FEBS Lett. 405:1997;81-85.
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(1997)
FEBS Lett
, vol.405
, pp. 81-85
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Pan, P.1
Bayley, H.2
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25
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0031260274
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Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins
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Gallivan JP, Lester HA, Dougherty DA Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins. Chem Biol. 4:1997;739-749.
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Chem Biol
, vol.4
, pp. 739-749
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Gallivan, J.P.1
Lester, H.A.2
Dougherty, D.A.3
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26
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0032055921
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Flash decaging of tyrosine sidechains in an ion channel
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In this and related papers, the Caltech researchers apply non-natural amino acid mutagenesis to make modified eukaryotic ion channels in oocytes. Here, tyrosine with a photoremovable protecting group is introduced at a key position in the a subunit of the ligand-gated acetylcholine receptor, producing a channel protein that can be activated by light. Similar technology might be applied to the in vitro synthesis of a variety of modified channels and pores.
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Miller JC, Silverman SK, England PM, Dougherty DA, Lester HA Flash decaging of tyrosine sidechains in an ion channel. Neuron. 20:1998;619-624. In this and related papers, the Caltech researchers apply non-natural amino acid mutagenesis to make modified eukaryotic ion channels in oocytes. Here, tyrosine with a photoremovable protecting group is introduced at a key position in the a subunit of the ligand-gated acetylcholine receptor, producing a channel protein that can be activated by light. Similar technology might be applied to the in vitro synthesis of a variety of modified channels and pores.
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(1998)
Neuron
, vol.20
, pp. 619-624
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Miller, J.C.1
Silverman, S.K.2
England, P.M.3
Dougherty, D.A.4
Lester, H.A.5
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27
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0030923523
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Site-specific, photochemical proteolysis applied to ion channels in vivo
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England PM, Lester HA, Davidson N, Dougherty DA Site-specific, photochemical proteolysis applied to ion channels in vivo. Proc Natl Acad Sci USA. 94:1997;11025-11030.
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Proc Natl Acad Sci USA
, vol.94
, pp. 11025-11030
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England, P.M.1
Lester, H.A.2
Davidson, N.3
Dougherty, D.A.4
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28
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0031322936
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Biosynthetic systems for nonribosomal antibiotic assembly
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Mootz HD, Marahiel MA Biosynthetic systems for nonribosomal antibiotic assembly. Curr Opin Chem Biol. 1:1997;543-551.
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Curr Opin Chem Biol
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, pp. 543-551
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Mootz, H.D.1
Marahiel, M.A.2
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29
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0032475992
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Harnessing the biosynthetic code-combinations, permutations, and mutations
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Hybrid modular synthetases have been heavily exploited for the synthesis of various natural products, especially the polyketides. It is possible that a vast array of channel-forming peptides could be produced by similar means.
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Cane DE, Walsh CT, Khosla C Harnessing the biosynthetic code-combinations, permutations, and mutations. Science. 282:1998;63-68. Hybrid modular synthetases have been heavily exploited for the synthesis of various natural products, especially the polyketides. It is possible that a vast array of channel-forming peptides could be produced by similar means.
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(1998)
Science
, vol.282
, pp. 63-68
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Cane, D.E.1
Walsh, C.T.2
Khosla, C.3
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30
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0029971826
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Engineering stabilized ion channels - covalent dimers of alamethicin
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You SC, Peng SY, Lien L, Breed J, Sansom MSP, Woolley GA Engineering stabilized ion channels - covalent dimers of alamethicin. Biochemistry. 35:1996;6225-6232.
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Biochemistry
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You, S.C.1
Peng, S.Y.2
Lien, L.3
Breed, J.4
Sansom, M.S.P.5
Woolley, G.A.6
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31
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0001073480
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Supramolecular design by covalent capture. Design of a peptide cylinder via hydrogen-bond-promoted intermolecular olefin metathesis
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Clark TD, Ghadiri MR Supramolecular design by covalent capture. Design of a peptide cylinder via hydrogen-bond-promoted intermolecular olefin metathesis. J Am Chem Soc. 117:1995;12364-12365.
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Mutter M, Tuchscherer G Non-native architectures in protein design and mimicry. Cellular Molec Life Sci. 53:1997;851-863.
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Cellular Molec Life Sci
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Mutter, M.1
Tuchscherer, G.2
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33
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0030867021
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Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeats I-IV) of the sodium channel
-
Four different synthetic helices based on sodium channel sequences were attached at specific positions to a peptide template. The assembled helices exhibited channel activity; however, it is unlikely that this results from any resemblance to the natural channel structure. At this stage, the work is most notable for the synthetic methodology, which might be further exploited with respect for new knowledge about channel structure and function.
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Futaki S, Aoki M, Fukuda M, Kondo F, Niwa M, Kitagawa K, Nakaya Y Assembling of the four individual helices corresponding to the transmembrane segments (S4 in repeats I-IV) of the sodium channel. Tetrahedron Lett. 38:1997;7071-7074. Four different synthetic helices based on sodium channel sequences were attached at specific positions to a peptide template. The assembled helices exhibited channel activity; however, it is unlikely that this results from any resemblance to the natural channel structure. At this stage, the work is most notable for the synthetic methodology, which might be further exploited with respect for new knowledge about channel structure and function.
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Tetrahedron Lett
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, pp. 7071-7074
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Futaki, S.1
Aoki, M.2
Fukuda, M.3
Kondo, F.4
Niwa, M.5
Kitagawa, K.6
Nakaya, Y.7
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34
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0032932083
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Crystal structure of staphyococcal lukF delineates conformational changes accompanying formation of a transmembrane channel
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in press. LukF is homologous to staphylococcal α-hemolysin, for which the structure of the fully assembled heptameric transmembrane pore has been determined. Therefore, this structure of a water-soluble monomer provides insight into the assembly process with atomic detail. Information such as this is invaluable for the rational design of self assembling channels and pores
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Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E: Crystal structure of staphyococcal lukF delineates conformational changes accompanying formation of a transmembrane channel. Nat Struct Biol 1999, in press. LukF is homologous to staphylococcal α-hemolysin, for which the structure of the fully assembled heptameric transmembrane pore has been determined. Therefore, this structure of a water-soluble monomer provides insight into the assembly process with atomic detail. Information such as this is invaluable for the rational design of self assembling channels and pores.
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(1999)
Nat Struct Biol
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Olson, R.1
Nariya, H.2
Yokota, K.3
Kamio, Y.4
Gouaux, E.5
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35
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0029924449
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Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin
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Valeva A, Weisser A, Walker B, Kehoe M, Bayley H, Bhakdi S, Palmer M Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin. EMBO J. 15:1996;1857-1864.
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EMBO J
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, pp. 1857-1864
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Valeva, A.1
Weisser, A.2
Walker, B.3
Kehoe, M.4
Bayley, H.5
Bhakdi, S.6
Palmer, M.7
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36
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0031404458
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Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β barrel
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Cheley S, Malghani MS, Song L, Hobaugh M, Gouaux JE, Yang J, Bayley H Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β barrel. Protein Eng. 10:1997;1433-1443.
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Protein Eng
, vol.10
, pp. 1433-1443
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Cheley, S.1
Malghani, M.S.2
Song, L.3
Hobaugh, M.4
Gouaux, J.E.5
Yang, J.6
Bayley, H.7
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37
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0030974351
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Electrostatic effects on ion selectivity and rectification in designed ion channel peptides
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Lear JD, Schneider JP, Kienker PK, DeGrado WF Electrostatic effects on ion selectivity and rectification in designed ion channel peptides. J Am Chem Soc. 119:1997;3212-3217.
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J Am Chem Soc
, vol.119
, pp. 3212-3217
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Lear, J.D.1
Schneider, J.P.2
Kienker, P.K.3
Degrado, W.F.4
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39
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0031554429
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A biosensor that uses ion-channel switches
-
Tethered supported bilayers containing the channel-forming gramicidin A peptide have been made that respond to large and small analytes, which alter the density of open channels. It has proved difficult to place functional channels in supported bilayers and the work is distinguished in this regard. However, while the devices are robust, versatile and highly sensitive, they are complex assemblies, which would benefit from simplification.
-
Cornell BA, Braach-Maksvytis VLB, King LG, Osman PDJ, Raguse B, Wieczorek L, Pace RJ A biosensor that uses ion-channel switches. Nature. 387:1997;580-583. Tethered supported bilayers containing the channel-forming gramicidin A peptide have been made that respond to large and small analytes, which alter the density of open channels. It has proved difficult to place functional channels in supported bilayers and the work is distinguished in this regard. However, while the devices are robust, versatile and highly sensitive, they are complex assemblies, which would benefit from simplification.
-
(1997)
Nature
, vol.387
, pp. 580-583
-
-
Cornell, B.A.1
Braach-Maksvytis, V.L.B.2
King, L.G.3
Osman, P.D.J.4
Raguse, B.5
Wieczorek, L.6
Pace, R.J.7
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Supported membranes: Scientific and practical applications
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Sackmann E Supported membranes: scientific and practical applications. Science. 271:1996;43-48.
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Science
, vol.271
, pp. 43-48
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Sackmann, E.1
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41
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0032070193
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Impedance spectroscopy of porin and gramicidin pores reconstituted into supported bilayers on indium-tin-oxide electrodes
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Gritsch S, Nollert P, Jähnig F, Sackmann E Impedance spectroscopy of porin and gramicidin pores reconstituted into supported bilayers on indium-tin-oxide electrodes. Langmuir. 14:1998;3118-3125.
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Langmuir
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Gritsch, S.1
Nollert, P.2
Jähnig, F.3
Sackmann, E.4
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42
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0032477653
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Tethered lipid bilayer membranes - formation and ionic reservoir characterization
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Raguse B, Braach-Maksvytis V, Cornell BA, King LG, Osman PDJ, Pace RJ, Wieczorek L Tethered lipid bilayer membranes - formation and ionic reservoir characterization. Langmuir. 14:1998;648-659.
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Langmuir
, vol.14
, pp. 648-659
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Raguse, B.1
Braach-Maksvytis, V.2
Cornell, B.A.3
King, L.G.4
Osman, P.D.J.5
Pace, R.J.6
Wieczorek, L.7
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43
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0032513708
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Oriented self-assembly of cyclic peptide nanotubes in lipid membranes
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Kim HS, Hartgerink JD, Ghadiri MR Oriented self-assembly of cyclic peptide nanotubes in lipid membranes. J Am Chem Soc. 120:1998;4417-4424.
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J Am Chem Soc
, vol.120
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Kim, H.S.1
Hartgerink, J.D.2
Ghadiri, M.R.3
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44
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1842410757
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Diffusion-limited size-selective ion sensing based on SAM-supported peptide nanotubes
-
Peptide nanotubes were incorporated into monolayers supported on a gold surface. The 7.5 Å diameter of the channels dictated the accessibility of the gold surface to electroactive ions. The work therefore forms the basis of a rugged sensor based on size selectivity as well as electrochemistry.
-
Motesharei K, Ghadiri MR Diffusion-limited size-selective ion sensing based on SAM-supported peptide nanotubes. J Am Chem Soc. 119:1997;11306-11312. Peptide nanotubes were incorporated into monolayers supported on a gold surface. The 7.5 Å diameter of the channels dictated the accessibility of the gold surface to electroactive ions. The work therefore forms the basis of a rugged sensor based on size selectivity as well as electrochemistry.
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(1997)
J Am Chem Soc
, vol.119
, pp. 11306-11312
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Motesharei, K.1
Ghadiri, M.R.2
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45
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0032513080
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Self-assembled α-hemolysin pores in an S-layer supported lipid bilayer
-
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