ライフサイエンスコーパス: gramicidin A

1 tion kinetics of the channel-forming peptide gramicidin A.

2 n receptor (ASGR), and an antibiotic peptide gramicidin A.

3 rivatives of the ion-channel-forming peptide gramicidin A.

4 ugh pores of the ion channel-forming peptide gramicidin A.

5 f ions through prototypical channels such as gramicidin A.

6 -to-end dimer and double-helix structures of gramicidin A.

7 abeled backbone sites (Trp13, Val7, Gly2) in gramicidin A.

8 tly different from those formed by the ester gramicidin A.

9 een recorded for each of the four indoles of gramicidin A.

10 nel-forming proteins, such as aquaporins and gramicidin-A.

11 of depths in membrane systems is applied to gramicidin A, a membrane-bound peptide of known structur

12 using experimental solid-state NMR data from gramicidin A, a monovalent cation channel in lipid bilay

13 lays no clinical role in general anesthesia, gramicidin A, a transmembrane channel peptide, provides

14 tors incorporate transmembrane peptide pores gramicidin A and alamethicin in the lipid bilayer they c

15 mer or doubly charged monomer of the peptide gramicidin A and conformers of the [M + 5H](5+) form of

16 rent-voltage relations of (5F-Indole)Trp(13) gramicidin A and gramicidin A channels (, 75:2830-2844).

17 ublished homodimer conductance data for both gramicidin A and gramicidin M channels confirms this con

18 shable populations about halfway between the gramicidin A and gramicidin M homodimer conductances.

19 implies that the principle difference in the gramicidin A and gramicidin M transport free-energy prof

20 elated to the free-energy difference between gramicidin A and gramicidin M, we construct an effective

21 H(3)0+, on the structure of the ion channel gramicidin A and the hydrogen-bonded network of waters w

22 ture of the channels when compared to native gramicidin A, and only small effects are seen on side-ch

23 (1)H spin diffusion experiments on unlabeled gramicidin A are sufficient to discriminate between the

24 om molecular dynamics simulations (MD) using gramicidin A as a prototypical narrow ion channel.

25 Using gramicidin A as a simplified model for transmembrane ion

26 ated relative single-channel conductances of gramicidin A, B, and C agree well with experiment.

27 Gramicidins A, B, and C are the three most abundant, nat

28 he peptide bond between Val(1) and Gly(2) in gramicidin A by an ester bond.

29 ced cytotoxicity and direct Na(+) loading by gramicidin-A caused Pico145-resistant cytotoxicity in th

30 he mobility of protons in a dioxolane-linked gramicidin A channel (D1) is comparable to the mobility

31 ferent stereoisomers of the dioxolane-linked gramicidin A channel (the SS and RR dimers) were measure

32 concentrations of HCl, proton mobilities in gramicidin A channel and in solution differ by only 25%.

33 Using a cation-selective gramicidin A channel as a sensor of the membrane surface

34 er surface charge and gauge its influence on gramicidin A channel conductance by two strategies: titr

35 to electrostatic effects of surface charge, gramicidin A channel conductance is also influenced by l

36 rifluorocyclobutane (F3), was found to alter gramicidin A channel function by enhancing Na(+) transpo

37 Through the high-resolution structure of the gramicidin A channel in lamellar phase lipids and the ch

38 The PMF profile of the ion along the Gramicidin A channel is obtained by combining an equilib

39 ifluorocyclobutane causes minimal changes in gramicidin A channel structure in sodium dodecyl sulfate

40 d closing of the monovalent cation selective gramicidin A channel through single channel conductance,

41 we consider ion permeation energetics in the gramicidin A channel using a novel polarizable force fie

42 cantly affect the secondary structure of the gramicidin A channel.

43 have been proposed for the membrane-spanning gramicidin A channel: one based on solid-state NMR exper

44 tions of (5F-Indole)Trp(13) gramicidin A and gramicidin A channels (, 75:2830-2844).

45 Gramicidin A channels are miniproteins that are anchored

46 Using gramicidin A channels as a tool to probe bilayer mechani

47 re the consequences of lipid diversity using gramicidin A channels embedded in phosphatidylcholine (P

48 concluded that 1) The mobility of protons in gramicidin A channels in different lipid bilayers is rem

49 ) Differences between proton conductances in gramicidin A channels in GMO and PEPC cannot be explaine

50 we study the effect of Hofmeister anions on gramicidin A channels in lipid membranes.

51 ree energy governing K(+) conduction through gramicidin A channels is characterized by using over 0.1

52 re and/or dynamics of water molecules inside gramicidin A channels is modulated by the lipid environm

53 We find that the sensitivity of gramicidin A channels to the anesthetic halothane is hig

54 iology, is analyzed in side-chain analogs of gramicidin A channels.

55 ryptophan substitutions in membrane-spanning gramicidin A channels.

56 eplacements on the structure and function of gramicidin A channels.

57 channel permeability, we designed different gramicidin A derivatives with attached acyl chains.

58 Inclusion of a gramicidin A dimer (approximately 1 mol %) yields simila

59 A study of ion transport through gramicidin A dimer is carried out within this PNP framew

60 The most commonly observed and most stable gramicidin A dimer is the main object of this study.

61 Unlike dioleoyl phosphatidylethanolamine and gramicidin A-DOPC, small-angle x-ray scattering and (31)

62 tions, dioleoyl phosphatidylethanolamine and gramicidin A-DOPC, which form the negatively curved hexa

63 lular membrane with the liposomes containing gramicidin A forming cation-conductive beta-helix in the

64 across an SLB incorporating the ion channels Gramicidin A (gA) and Alamethicin (ALM).

65 Two canonical dynamic ion channels (gramicidin A (gA) and alamethicin) and one static biolog

66 ts on the transfer of protons in both native gramicidin A (gA) and in covalently linked SS- and RR-di

67 ces to protons (g(H)) were studied in native gramicidin A (gA) and in the SS and RR diastereoisomers

68 channel proton conductances (g(H)) in native gramicidin A (gA) and in two diastereoisomers (SS and RR

69 "spacer" residues between the tryptophans in gramicidin A (gA) are important for channel structure an

70 n the central valine residues 6, 7, and 8 of gramicidin A (gA) are shifted by one position, the resul

71 xamined the effect of GsMTx4 and enGsMTx4 on gramicidin A (gA) channel gating.

72 lar dynamics simulations were performed on a gramicidin A (gA) channel in a fully hydrated dimyristoy

73 ts of halothane, a clinical anesthetic, on a gramicidin A (gA) channel in a fully hydrated dimyristoy

74 The four Trp dipoles in the gramicidin A (gA) channel modulate channel conductance,

75 To overcome this problem, we use gramicidin A (gA) channels as molecular force probes to

76 mechanism and examined genistein's effect on gramicidin A (gA) channels in planar phospholipid bilaye

77 The dissociation of gramicidin A (gA) channels into monomers is the simplest

78 dipole moment of the four Trp side chains in gramicidin A (gA) channels modify channel conductance th

79 ferent stereoisomers of the dioxolane-linked gramicidin A (gA) channels reconstituted in planar lipid

80 ferent stereoisomers of the dioxolane-linked gramicidin A (gA) channels were individually synthesized

81 single SS stereoisomers of dioxolane-linked gramicidin A (gA) channels were measured in different ph

82 of the four tryptophans of membrane-spanning gramicidin A (gA) channels, the inclusion of the perpend

83 ith conductances that are lower than that of gramicidin A (gA) channels.

84 rried out coarse-grained (CG) simulations of gramicidin A (gA) dimer association and analyzed the res

85 the three-dimensional stress field around a gramicidin A (gA) dimer in lipid bilayers that feature d

86 ly kinetics and conformer preferences of the gramicidin A (GA) dimer is investigated using a combinat

87 The conformational preferences adopted by gramicidin A (GA) dimers inserted into phospholipid bila

88 ize the volatile anesthetic binding sites in gramicidin A (gA) incorporated into sodium dodecyl sulfa

89 be the solution phase structure of dimerized Gramicidin A (GA) inserted into lipid vesicle bilayers i

90 -resonance (2D-FT-ESR) to the study of lipid/gramicidin A (GA) interactions is reported.

91 Embedded gramicidin A (gA) ionchannels in a self-assembled tether

92 Gramicidin A (gA) is a 15-amino-acid antibiotic peptide

93 Gramicidin A (gA) molecules were covalently linked with

94 ata set for homodimeric channels formed from gramicidin A (gA) or any of eight fluorinated Trp analog

95 as replaced by Ser at position 3 or 5 in the gramicidin A (gA) sequence: formyl-VG(2)A(3)LA(5)VVVWLWL

96 le ion channel conductance of derivatives of gramicidin A (gA) upon reaction with analytes in solutio

97 the gel state) containing various amounts of gramicidin A (gA) were imaged in aqueous solutions and a

98 rom labeled tryptophans in membrane-spanning gramicidin A (gA)(1) channels to refine the geometry of

99 protons in water wires was studied in native gramicidin A (gA), and in the SS- and RR-diastereoisomer

100 of measurements of proton conduction through gramicidin A (gA), B (gB), and M (gM) homodimer channels

101 The ion channel, gramicidin A (gA), houses within its helical structure j

102 Gramicidin A (gA), with four Trp residues per monomer, h

103 gallate (nPG)--on bilayer properties using a gramicidin A (gA)-based fluorescence quench assay to pro

104 bilayer properties using channels formed by gramicidin A (gA).

105 oxygen of transmembrane pore-forming peptide gramicidin A (gA).

106 In this study, new covalently linked gramicidin-A (gA) peptides were synthesized, and the eff

107 ndary lipid in membrane vesicles of DPPC and gramicidin A' (GA) is reported.

108 The effect of aggregation of gramicidin A' (GA) on the phase structure of dipalmitoyl

109 Gramicidin A(gA) can be palmitoylated by means of an est

110 utions were introduced into the enantiomeric gramicidin A-, gA-.) Circular dichroism spectra of [D-Al

111 Gramicidin A/gramicidin M heterodimer conductances were

112 channel formed by a dimer of the polypeptide gramicidin A has a single-stranded, right-handed helical

113 n of the gramicidin channel, four analogs of gramicidin A have been synthesized in which the tryptoph

114 ld slower in gramicidin M homodimers than in gramicidin A homodimers and that first- and second-ion e

115 t claim, the solid-state NMR constraints for gramicidin A in a lipid bilayer are not consistent with

116 hree-dimensional continuum elastic model for gramicidin A in a lipid bilayer is shown to describe the

117 With 400 microM gramicidin A in a vesicle suspension of 60 mM phosphatid

118 m transport study showed that with 75 microM gramicidin A in a vesicle suspension of 66 mM PC/PG, F3

119 Analogues of gramicidin A in which the Trp residues at positions 9, 1

120 age relations for ion permeation through the gramicidin A ion channel embedded in membranes character

121 h is utilized to predict current through the Gramicidin A ion channel, a narrow pore in which the app

122 ramework model for proton conduction through gramicidin; a model designed to incorporate information

123 yers, modulate the structurally well-defined gramicidin A monomer <--> dimer reaction.

124 Addition of the transmembrane protein gramicidin A or construction of a highly defected gel ph

125 by Na(+),K(+)-ATPase with subtoxic doses of gramicidin A or ouabain.

126 meric state has been observed for the native gramicidin A peptide.

127 For gramicidin, a single laser shot UVPD discriminates betwe

128 the conductance of the pore-forming peptide gramicidin A to monitor PLD activity, the work presented

129 l as hydrophilic defects and the ion channel gramicidin A, to provide parallels to membranes deformed

130 Gramicidin A was studied by continuous wave electron spi

131 k lipid membranes (BLMs) functionalized with gramicidin A were conducted using a fast perfusion syste

132 Moreover, the carbonyl groups of gramicidin A were found to interact with the charge on t

133 a backbone fold identical to that of native gramicidin A, with only small changes in the side chain