1bh1

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[[Image:1bh1.png|left|200px]]
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==STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES==
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<StructureSection load='1bh1' size='340' side='right' caption='[[1bh1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BH1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh1 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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D-Pro14 melittin was synthesized to investigate the effect of increasing the angle of the bend in the hinge region between the helical segments of the molecule. Structural analysis by nuclear magnetic resonance indicated that, in methanol, the molecule consisted of two helices separated at Pro14, as in melittin. However, the two helices in D-Pro14 melittin were laterally displaced relative to each other by approximately 7 A, and in addition, there was a small rotation of the carboxyl-terminal helix relative to the amino-terminal helix around the long axis of the molecule. The peptide had less than 5% of the cytolytic activity of melittin. Modification of Arg22 with the 2,2,5,7,8-pentamethyl-chroman-6-sulphonyl (pmc) group restored hemolytic activity to close to that of unmodified melittin. Replacement of Arg22 with Phe was less effective in restoring hemolytic activity. Electron-paramagnetic resonance studies suggest that there is a positive correlation between hemolytic activity of the peptides and interaction with phospholipid bilayers.
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{{STRUCTURE_1bh1| PDB=1bh1 | SCENE= }}
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Structure and activity of D-Pro14 melittin.,Hewish DR, Barnham KJ, Werkmeister JA, Kirkpatrick A, Bartone N, Liu ST, Norton RS, Curtain C, Rivetta DE J Protein Chem. 2002 May;21(4):243-53. PMID:12168695<ref>PMID:12168695</ref>
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===STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12168695}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1bh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH1 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012168695</ref><references group="xtra"/>
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[[Category: Apis mellifera]]
[[Category: Apis mellifera]]
[[Category: Barnham, K J.]]
[[Category: Barnham, K J.]]

Revision as of 05:50, 8 June 2014

STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES

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