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-[[Image:1nt5.jpg|left|200px]]<br /><applet load="1nt5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nt5.jpg|left|200px]]<br /><applet load="1nt5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nt5" />
 '''F1-Gramicidin A in Sodium Dodecyl Sulfate Micelles (NMR)'''<br />
 ==Overview==
-To further investigate the effect of single amino acid substitution on the, structure and function of the gramicidin channel, an analogue of, gramicidin A (GA) has been synthesized in which Trp(15) is replaced by Gly, in the critical aqueous interface and cation binding region. The structure, of Gly(15)-GA incorporated into SDS micelles has been determined using a, combination of 2D-NMR spectroscopy and molecular modeling. Like the parent, GA, Gly(15)-GA forms a dimeric channel composed of two single-stranded, right-handed beta(6.3)-helices joined by hydrogen bonds between their, N-termini. The replacement of Trp(15) by Gly does not have a significant, effect on backbone structure or side chain conformations with the, exception of Trp(11) in which the indole ring is rotated away from the, channel axis. Measurement of the equilibrium binding constants and Delta G, for the binding of monovalent cations to GA and Gly(15)-GA channels, incorporated into PC vesicles using (205)Tl NMR spectroscopy shows that, monovalent cations bind much more weakly to the Gly(15)-GA channel, entrance than to GA channels. Utilizing the magnetization inversion, transfer NMR technique, the transport of Na(+) ions through GA and, Gly(15)-GA channels incorporated into PC/PG vesicles has been, investigated. The Gly(15) substitution produces an increase in the, activation enthalpy of transport and thus a significant decrease in the, transport rate of the Na(+) ion is observed. The single-channel, appearances show that the conducting channels have a single, well-defined, structure. Consistent with the NMR results, the single-channel, conductances are reduced by 30% and the lifetimes by 70%. It is concluded, that the decrease in cation binding, transport, and conductance in, Gly(15)-GA results from the removal of the Trp(15) dipole and, to a lesser, extent, the change in orientation of Trp(11).
+To further investigate the effect of single amino acid substitution on the structure and function of the gramicidin channel, an analogue of gramicidin A (GA) has been synthesized in which Trp(15) is replaced by Gly in the critical aqueous interface and cation binding region. The structure of Gly(15)-GA incorporated into SDS micelles has been determined using a combination of 2D-NMR spectroscopy and molecular modeling. Like the parent GA, Gly(15)-GA forms a dimeric channel composed of two single-stranded, right-handed beta(6.3)-helices joined by hydrogen bonds between their N-termini. The replacement of Trp(15) by Gly does not have a significant effect on backbone structure or side chain conformations with the exception of Trp(11) in which the indole ring is rotated away from the channel axis. Measurement of the equilibrium binding constants and Delta G for the binding of monovalent cations to GA and Gly(15)-GA channels incorporated into PC vesicles using (205)Tl NMR spectroscopy shows that monovalent cations bind much more weakly to the Gly(15)-GA channel entrance than to GA channels. Utilizing the magnetization inversion transfer NMR technique, the transport of Na(+) ions through GA and Gly(15)-GA channels incorporated into PC/PG vesicles has been investigated. The Gly(15) substitution produces an increase in the activation enthalpy of transport and thus a significant decrease in the transport rate of the Na(+) ion is observed. The single-channel appearances show that the conducting channels have a single, well-defined structure. Consistent with the NMR results, the single-channel conductances are reduced by 30% and the lifetimes by 70%. It is concluded that the decrease in cation binding, transport, and conductance in Gly(15)-GA results from the removal of the Trp(15) dipole and, to a lesser extent, the change in orientation of Trp(11).
 ==About this Structure==
-NT5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with FOR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NT5 OCA].
+NT5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=FOR:'>FOR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT5 OCA].
 ==Reference==
 The structure, cation binding, transport, and conductance of Gly15-gramicidin A incorporated into SDS micelles and PC/PG vesicles., Sham SS, Shobana S, Townsley LE, Jordan JB, Fernandez JQ, Andersen OS, Greathouse DV, Hinton JF, Biochemistry. 2003 Feb 18;42(6):1401-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12578352 12578352]
 [[Category: Protein complex]]
-[[Category: Fletcher, T.G.]]
+[[Category: Fletcher, T G.]]
-[[Category: Hinton, J.F.]]
+[[Category: Hinton, J F.]]
-[[Category: Townsley, L.E.]]
+[[Category: Townsley, L E.]]
 [[Category: FOR]]
-[[Category: beta-6.3 helix]]
+[[Category: beta-6 3 helix]]
 [[Category: linear gramicidin]]
 [[Category: membrane ion channel]]
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 [[Category: single-stranded helical dimer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:45:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:41 2008''