4nj0
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==GCN4-p1 single Val9 to Ile mutant== |
| + | <StructureSection load='4nj0' size='340' side='right' caption='[[4nj0]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4nj0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NJ0 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dmd|4dmd]], [[2zta|2zta]], [[4niz|4niz]], [[4nj1|4nj1]], [[4nj2|4nj2]]</td></tr> | ||
| + | <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=4nj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nj0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nj0 RCSB], [http://www.ebi.ac.uk/pdbsum/4nj0 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nature uses proteins and nucleic acids to form a wide array of functional architectures, and scientists have found inspiration from these structures in the rational design of synthetic biomaterials. We have recently shown that a modular subunit consisting of two alpha-helical coiled coil peptides attached at their midpoints by an organic linking group can spontaneously self-assemble in aqueous solution to form a soluble supramolecular polymer. Here we explore the use of coiled-coil association affinity, readily tuned by amino acid sequence, as a means to predictably alter properties of these supramolecular assemblies. A series of dimeric coiled-coil peptide sequences with identical quaternary folded structures but systematically altered folded stability were designed and biophysically characterized. The sequences were cross-linked to generate a series of branched, self-assembling biomacromolecular subunits. A clear relationship is observed between coiled-coil association affinity and apparent hydrodynamic diameter of the supramolecular polymers formed by these subunits. Our results provide a family of soluble supramolecular polymers of tunable size and well-characterized coiled-coil sequences that add to the library of building blocks available for use in the rational design of protein-based supramolecular biomaterials. | ||
| - | + | Tuning assembly size in Peptide-based supramolecular polymers by modulation of subunit association affinity.,Oshaben KM, Horne WS Biomacromolecules. 2014 Apr 14;15(4):1436-42. doi: 10.1021/bm5000423. Epub 2014, Mar 17. PMID:24598042<ref>PMID:24598042</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Horne, W S.]] | ||
| + | [[Category: Oshaben, K M.]] | ||
| + | [[Category: Transcription]] | ||
Revision as of 16:22, 20 August 2014
GCN4-p1 single Val9 to Ile mutant
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