1fct: Difference between revisions

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[[Image:1fct.gif|left|200px]]<br /><applet load="1fct" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1fct.gif|left|200px]]<br /><applet load="1fct" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1fct" />

'''NMR STRUCTURES OF FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE FROM CHLAMYDOMONAS REINHARDTII PROMOTED BY TRIFLUOROETHANOL IN AQUEOUS SOLUTION'''<br />

==Overview==

The 32-amino acid transit peptide of the unicellular green alga, Chlamydomonas reinhardtii ferredoxin has been synthesized and analysed by, NMR spectroscopy and circular dichroism. The results show that while the, peptide is unstructured in water, it undergoes an alpha-helix formation, from residue 3 to 13 in a 30:70 molar-ratio mixture of, 2,2,2-trifluoroethanol. The remainder of the peptide is still unstructured, in CF3CD2OD/H2O mixtures, but is distributed on a side opposite to a, hydrophobic ridge formed by Met5, Phe9 and Val13 on the induced, alpha-helix. The NMR structures driven by 2,2,2-trifluoroethanol in, aqueous solution, are discussed in terms of potent interactions with the, chloroplast envelope and its translocation molecular machinery.

The 32-amino acid transit peptide of the unicellular green alga Chlamydomonas reinhardtii ferredoxin has been synthesized and analysed by NMR spectroscopy and circular dichroism. The results show that while the peptide is unstructured in water, it undergoes an alpha-helix formation from residue 3 to 13 in a 30:70 molar-ratio mixture of 2,2,2-trifluoroethanol. The remainder of the peptide is still unstructured in CF3CD2OD/H2O mixtures, but is distributed on a side opposite to a hydrophobic ridge formed by Met5, Phe9 and Val13 on the induced alpha-helix. The NMR structures driven by 2,2,2-trifluoroethanol in aqueous solution, are discussed in terms of potent interactions with the chloroplast envelope and its translocation molecular machinery.

==About this Structure==

1FCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FCT OCA].

1FCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCT OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Blackledge, M.]]

[[Category: Lancelin, J.M.]]

[[Category: Lancelin, J M.]]

[[Category: transit peptide]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 14~~:49:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:21 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1fct.gif|left|200px]]<br /><applet load="1fct" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fct.gif|left|200px]]<br /><applet load="1fct" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fct" />
 '''NMR STRUCTURES OF FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE FROM CHLAMYDOMONAS REINHARDTII PROMOTED BY TRIFLUOROETHANOL IN AQUEOUS SOLUTION'''<br />
 ==Overview==
-The 32-amino acid transit peptide of the unicellular green alga, Chlamydomonas reinhardtii ferredoxin has been synthesized and analysed by, NMR spectroscopy and circular dichroism. The results show that while the, peptide is unstructured in water, it undergoes an alpha-helix formation, from residue 3 to 13 in a 30:70 molar-ratio mixture of, 2,2,2-trifluoroethanol. The remainder of the peptide is still unstructured, in CF3CD2OD/H2O mixtures, but is distributed on a side opposite to a, hydrophobic ridge formed by Met5, Phe9 and Val13 on the induced, alpha-helix. The NMR structures driven by 2,2,2-trifluoroethanol in, aqueous solution, are discussed in terms of potent interactions with the, chloroplast envelope and its translocation molecular machinery.
+The 32-amino acid transit peptide of the unicellular green alga Chlamydomonas reinhardtii ferredoxin has been synthesized and analysed by NMR spectroscopy and circular dichroism. The results show that while the peptide is unstructured in water, it undergoes an alpha-helix formation from residue 3 to 13 in a 30:70 molar-ratio mixture of 2,2,2-trifluoroethanol. The remainder of the peptide is still unstructured in CF3CD2OD/H2O mixtures, but is distributed on a side opposite to a hydrophobic ridge formed by Met5, Phe9 and Val13 on the induced alpha-helix. The NMR structures driven by 2,2,2-trifluoroethanol in aqueous solution, are discussed in terms of potent interactions with the chloroplast envelope and its translocation molecular machinery.
 ==About this Structure==
-FCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FCT OCA].
+FCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCT OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Blackledge, M.]]
-[[Category: Lancelin, J.M.]]
+[[Category: Lancelin, J M.]]
 [[Category: transit peptide]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:49:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:21 2008''