1smz: Difference between revisions
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==Structure of Transportan in phospholipid bicellar solution== | |||
<StructureSection load='1smz' size='340' side='right'caption='[[1smz]]' scene=''> | |||
== Structural highlights == | |||
| | <table><tr><td colspan='2'>[[1smz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SMZ FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1smz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smz OCA], [https://pdbe.org/1smz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1smz RCSB], [https://www.ebi.ac.uk/pdbsum/1smz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1smz ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
''' | == Publication Abstract from PubMed == | ||
== | |||
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. | ||
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<ref>PMID:15178334</ref> | |||
NMR solution structure and position of transportan in neutral phospholipid bicelles., Barany-Wallje E, Andersson A, Graslund A, Maler L | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1smz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Andersson A]] | |||
[[Category: Barany-Wallje E]] | |||
[[Category: Graslund A]] | |||
[[Category: Maler L]] | |||
