1smz: Difference between revisions

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[[Image:1smz.~~gif~~|left|200px]]

[[Image:1smz.png|left|200px]]

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~~'''~~Structure of Transportan in phospholipid bicellar solution~~'''~~

===Structure of Transportan in phospholipid bicellar solution===

~~==Overview==~~

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Transportan is a chimeric cell-penetrating peptide constructed from the peptides galanin and mastoparan, which has the ability to internalize living cells carrying a hydrophilic load. In this study, we have determined the NMR solution structure and investigated the position of transportan in neutral bicelles. The structure revealed a well-~~defined alpha~~-~~helix in the C-terminal mastoparan part of the peptide and a weaker tendency to form an alpha-helix in the N-terminal domain.~~ The ~~position of the peptide in relation to the membrane~~, ~~as studied by adding paramagnetic probes~~, ~~shows that~~ the ~~peptide lies parallel~~ to~~, and in~~ the ~~head-group region of the membrane surface~~. ~~This result~~ is ~~supported by amide proton secondary chemical shifts~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15178334}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15178334 is the PubMed ID number.

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==About this Structure==

Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA].

Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA].

==Reference==

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[[Category: Maler, L.]]

[[Category: Transport protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 08~~:54:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:03:19 2008''

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-[[Image:1smz.gif|left|200px]]
+{{Seed}}
+[[Image:1smz.png|left|200px]]
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 {{STRUCTURE_1smz|  PDB=1smz  |  SCENE=  }}
-'''Structure of Transportan in phospholipid bicellar solution'''
+===Structure of Transportan in phospholipid bicellar solution===
-==Overview==
+<!--
-Transportan is a chimeric cell-penetrating peptide constructed from the peptides galanin and mastoparan, which has the ability to internalize living cells carrying a hydrophilic load. In this study, we have determined the NMR solution structure and investigated the position of transportan in neutral bicelles. The structure revealed a well-defined alpha-helix in the C-terminal mastoparan part of the peptide and a weaker tendency to form an alpha-helix in the N-terminal domain. The position of the peptide in relation to the membrane, as studied by adding paramagnetic probes, shows that the peptide lies parallel to, and in the head-group region of the membrane surface. This result is supported by amide proton secondary chemical shifts.
+The line below this paragraph, {{ABSTRACT_PUBMED_15178334}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15178334 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15178334}}
 ==About this Structure==
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA].
+Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA].
 ==Reference==
@@ Line 25: / Line 29: @@
 [[Category: Maler, L.]]
 [[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:54:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:03:19 2008''