This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1smz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1smz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1smz" /> '''Structure of Transportan in phospholipid bic...)
Line 1: Line 1:
-
[[Image:1smz.gif|left|200px]]<br /><applet load="1smz" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1smz.gif|left|200px]]<br /><applet load="1smz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1smz" />
caption="1smz" />
'''Structure of Transportan in phospholipid bicellar solution'''<br />
'''Structure of Transportan in phospholipid bicellar solution'''<br />
==Overview==
==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.
+
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.
==About this Structure==
==About this Structure==
-
1SMZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA].
+
1SMZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA].
==Reference==
==Reference==
Line 18: Line 18:
[[Category: transport protein]]
[[Category: transport protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:48:16 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:10 2008''

Revision as of 13:03, 21 February 2008


1smz

Drag the structure with the mouse to rotate

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.

About this Structure

1SMZ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

NMR solution structure and position of transportan in neutral phospholipid bicelles., Barany-Wallje E, Andersson A, Graslund A, Maler L, FEBS Lett. 2004 Jun 4;567(2-3):265-9. PMID:15178334

Page seeded by OCA on Thu Feb 21 15:03:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools