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1 een recorded for each of the four indoles of gramicidin A.
2 tion kinetics of the channel-forming peptide gramicidin A.
3 n receptor (ASGR), and an antibiotic peptide gramicidin A.
4 rivatives of the ion-channel-forming peptide gramicidin A.
5 ugh pores of the ion channel-forming peptide gramicidin A.
6 f ions through prototypical channels such as gramicidin A.
7 -to-end dimer and double-helix structures of gramicidin A.
8 abeled backbone sites (Trp13, Val7, Gly2) in gramicidin A.
9 tly different from those formed by the ester 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 otons at a rate 1.22 and 11 times as fast as gramicidin A and M2 channels, respectively, with excepti
22  H(3)0+, on the structure of the ion channel gramicidin A and the hydrogen-bonded network of waters w
23 ture of the channels when compared to native gramicidin A, and only small effects are seen on side-ch
24 (1)H spin diffusion experiments on unlabeled gramicidin A are sufficient to discriminate between the
25 om molecular dynamics simulations (MD) using gramicidin A as a prototypical narrow ion channel.
26                                        Using gramicidin A as a simplified model for transmembrane ion
27 ated relative single-channel conductances of gramicidin A, B, and C agree well with experiment.
28 hree ionophoric pentadecapeptide antibiotics gramicidin A, B, and C and their two corresponding isofo
29                                              Gramicidins A, B, and C are the three most abundant, nat
30 he peptide bond between Val(1) and Gly(2) in gramicidin A by an ester bond.
31 ced cytotoxicity and direct Na(+) loading by gramicidin-A caused Pico145-resistant cytotoxicity in th
32 he mobility of protons in a dioxolane-linked gramicidin A channel (D1) is comparable to the mobility
33 ferent stereoisomers of the dioxolane-linked gramicidin A channel (the SS and RR dimers) were measure
34  concentrations of HCl, proton mobilities in gramicidin A channel and in solution differ by only 25%.
35                     Using a cation-selective gramicidin A channel as a sensor of the membrane surface
36 er surface charge and gauge its influence on gramicidin A channel conductance by two strategies: titr
37  to electrostatic effects of surface charge, gramicidin A channel conductance is also influenced by l
38 rifluorocyclobutane (F3), was found to alter gramicidin A channel function by enhancing Na(+) transpo
39 Through the high-resolution structure of the gramicidin A channel in lamellar phase lipids and the ch
40         The PMF profile of the ion along the Gramicidin A channel is obtained by combining an equilib
41 ifluorocyclobutane causes minimal changes in gramicidin A channel structure in sodium dodecyl sulfate
42 d closing of the monovalent cation selective gramicidin A channel through single channel conductance,
43 we consider ion permeation energetics in the gramicidin A channel using a novel polarizable force fie
44 cantly affect the secondary structure of the gramicidin A channel.
45 have been proposed for the membrane-spanning gramicidin A channel: one based on solid-state NMR exper
46 tions of (5F-Indole)Trp(13) gramicidin A and gramicidin A channels (, 75:2830-2844).
47                                              Gramicidin A channels are miniproteins that are anchored
48                                        Using gramicidin A channels as a tool to probe bilayer mechani
49 re the consequences of lipid diversity using gramicidin A channels embedded in phosphatidylcholine (P
50 concluded that 1) The mobility of protons in gramicidin A channels in different lipid bilayers is rem
51 ) Differences between proton conductances in gramicidin A channels in GMO and PEPC cannot be explaine
52  we study the effect of Hofmeister anions on gramicidin A channels in lipid membranes.
53 ree energy governing K(+) conduction through gramicidin A channels is characterized by using over 0.1
54 re and/or dynamics of water molecules inside gramicidin A channels is modulated by the lipid environm
55              We find that the sensitivity of gramicidin A channels to the anesthetic halothane is hig
56 iology, is analyzed in side-chain analogs of gramicidin A channels.
57 ryptophan substitutions in membrane-spanning gramicidin A channels.
58 eplacements on the structure and function of gramicidin A channels.
59  channel permeability, we designed different gramicidin A derivatives with attached acyl chains.
60                               Inclusion of a gramicidin A dimer (approximately 1 mol %) yields simila
61             A study of ion transport through gramicidin A dimer is carried out within this PNP framew
62   The most commonly observed and most stable gramicidin A dimer is the main object of this study.
63 Unlike dioleoyl phosphatidylethanolamine and gramicidin A-DOPC, small-angle x-ray scattering and (31)
64 tions, dioleoyl phosphatidylethanolamine and gramicidin A-DOPC, which form the negatively curved hexa
65 lular membrane with the liposomes containing gramicidin A forming cation-conductive beta-helix in the
66 across an SLB incorporating the ion channels Gramicidin A (gA) and Alamethicin (ALM).
67          Two canonical dynamic ion channels (gramicidin A (gA) and alamethicin) and one static biolog
68 ts on the transfer of protons in both native gramicidin A (gA) and in covalently linked SS- and RR-di
69 ces to protons (g(H)) were studied in native gramicidin A (gA) and in the SS and RR diastereoisomers
70 channel proton conductances (g(H)) in native gramicidin A (gA) and in two diastereoisomers (SS and RR
71 "spacer" residues between the tryptophans in gramicidin A (gA) are important for channel structure an
72 n the central valine residues 6, 7, and 8 of gramicidin A (gA) are shifted by one position, the resul
73 xamined the effect of GsMTx4 and enGsMTx4 on gramicidin A (gA) channel gating.
74 lar dynamics simulations were performed on a gramicidin A (gA) channel in a fully hydrated dimyristoy
75 ts of halothane, a clinical anesthetic, on a gramicidin A (gA) channel in a fully hydrated dimyristoy
76                  The four Trp dipoles in the gramicidin A (gA) channel modulate channel conductance,
77             To overcome this problem, we use gramicidin A (gA) channels as molecular force probes to
78 mechanism and examined genistein's effect on gramicidin A (gA) channels in planar phospholipid bilaye
79                          The dissociation of gramicidin A (gA) channels into monomers is the simplest
80 dipole moment of the four Trp side chains in gramicidin A (gA) channels modify channel conductance th
81 ferent stereoisomers of the dioxolane-linked gramicidin A (gA) channels reconstituted in planar lipid
82 ferent stereoisomers of the dioxolane-linked gramicidin A (gA) channels were individually synthesized
83  single SS stereoisomers of dioxolane-linked gramicidin A (gA) channels were measured in different ph
84 of the four tryptophans of membrane-spanning gramicidin A (gA) channels, the inclusion of the perpend
85 ith conductances that are lower than that of gramicidin A (gA) channels.
86 rried out coarse-grained (CG) simulations of gramicidin A (gA) dimer association and analyzed the res
87  the three-dimensional stress field around a gramicidin A (gA) dimer in lipid bilayers that feature d
88 ly kinetics and conformer preferences of the gramicidin A (GA) dimer is investigated using a combinat
89    The conformational preferences adopted by gramicidin A (GA) dimers inserted into phospholipid bila
90 ize the volatile anesthetic binding sites in gramicidin A (gA) incorporated into sodium dodecyl sulfa
91 be the solution phase structure of dimerized Gramicidin A (GA) inserted into lipid vesicle bilayers i
92 -resonance (2D-FT-ESR) to the study of lipid/gramicidin A (GA) interactions is reported.
93            Electrophysiology measurements on gramicidin A (gA) ion channels embedded in planar suspen
94                                     Embedded gramicidin A (gA) ionchannels in a self-assembled tether
95                                              Gramicidin A (gA) is a 15-amino-acid antibiotic peptide
96                                              Gramicidin A (gA) molecules were covalently linked with
97 ata set for homodimeric channels formed from gramicidin A (gA) or any of eight fluorinated Trp analog
98 as replaced by Ser at position 3 or 5 in the gramicidin A (gA) sequence: formyl-VG(2)A(3)LA(5)VVVWLWL
99 le ion channel conductance of derivatives of gramicidin A (gA) upon reaction with analytes in solutio
100 the gel state) containing various amounts of gramicidin A (gA) were imaged in aqueous solutions and a
101 rom labeled tryptophans in membrane-spanning gramicidin A (gA)(1) channels to refine the geometry of
102 protons in water wires was studied in native gramicidin A (gA), and in the SS- and RR-diastereoisomer
103 of measurements of proton conduction through gramicidin A (gA), B (gB), and M (gM) homodimer channels
104                             The ion channel, gramicidin A (gA), houses within its helical structure j
105                                              Gramicidin A (gA), with four Trp residues per monomer, h
106 gallate (nPG)--on bilayer properties using a gramicidin A (gA)-based fluorescence quench assay to pro
107 ns and fluorescence-quenching experiments on gramicidin A (gA).
108  bilayer properties using channels formed by gramicidin A (gA).
109 oxygen of transmembrane pore-forming peptide gramicidin A (gA).
110         In this study, new covalently linked gramicidin-A (gA) peptides were synthesized, and the eff
111 ndary lipid in membrane vesicles of DPPC and gramicidin A' (GA) is reported.
112                 The effect of aggregation of gramicidin A' (GA) on the phase structure of dipalmitoyl
113                                              Gramicidin A(gA) can be palmitoylated by means of an est
114 utions were introduced into the enantiomeric gramicidin A-, gA-.) Circular dichroism spectra of [D-Al
115                                              Gramicidin A/gramicidin M heterodimer conductances were
116 channel formed by a dimer of the polypeptide gramicidin A has a single-stranded, right-handed helical
117 n of the gramicidin channel, four analogs of gramicidin A have been synthesized in which the tryptoph
118 ld slower in gramicidin M homodimers than in gramicidin A homodimers and that first- and second-ion e
119 t claim, the solid-state NMR constraints for gramicidin A in a lipid bilayer are not consistent with
120 hree-dimensional continuum elastic model for gramicidin A in a lipid bilayer is shown to describe the
121                              With 400 microM gramicidin A in a vesicle suspension of 60 mM phosphatid
122 m transport study showed that with 75 microM gramicidin A in a vesicle suspension of 66 mM PC/PG, F3
123                                 Analogues of gramicidin A in which the Trp residues at positions 9, 1
124 age relations for ion permeation through the gramicidin A ion channel embedded in membranes character
125 h is utilized to predict current through the Gramicidin A ion channel, a narrow pore in which the app
126  we report that lipid bilayers with embedded gramicidin A ion channels can structurally reorganize wh
127 ramework model for proton conduction through gramicidin; a model designed to incorporate information
128 yers, modulate the structurally well-defined gramicidin A monomer <--> dimer reaction.
129      Here, we demonstrate the wave nature of gramicidin, a natural antibiotic composed of 15 amino ac
130        Addition of the transmembrane protein gramicidin A or construction of a highly defected gel ph
131  by Na(+),K(+)-ATPase with subtoxic doses of gramicidin A or ouabain.
132 meric state has been observed for the native gramicidin A peptide.
133                                          For gramicidin, a single laser shot UVPD discriminates betwe
134  the conductance of the pore-forming peptide gramicidin A to monitor PLD activity, the work presented
135 l as hydrophilic defects and the ion channel gramicidin A, to provide parallels to membranes deformed
136                                              Gramicidin A was studied by continuous wave electron spi
137 k lipid membranes (BLMs) functionalized with gramicidin A were conducted using a fast perfusion syste
138             Moreover, the carbonyl groups of gramicidin A were found to interact with the charge on t
139  a backbone fold identical to that of native gramicidin A, with only small changes in the side chain

 
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