4tl1
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 9== |
| + | <StructureSection load='4tl1' size='340' side='right' caption='[[4tl1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tl1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TL1 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=02K:1-AMINOCYCLOHEXANECARBOXYLIC+ACID'>02K</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=4tl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tl1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tl1 RCSB], [http://www.ebi.ac.uk/pdbsum/4tl1 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Modular assembly of bio-inspired supramolecular polymers is a powerful technique to develop new soft nanomaterials, and protein folding is a versatile basis for preparing such materials. Previous work demonstrated a significant difference in the physical properties of closely related supramolecular polymers composed of building blocks in which identical coiled-coil forming peptides are cross-linked by one of two subtly different organic linkers (one flexible and the other rigid). Herein, we investigate the molecular basis for this observation by isolating a single subunit of the supramolecular polymer chain and probing its structure and conformational flexibility by double electron-electron resonance (DEER) spectroscopy. Experimental spin-spin distance distributions for two different labeling sites coupled with molecular dynamics simulations provide insights into how linker structure impacts chain dynamics in the coiled-coil supramolecular polymer. | ||
| - | + | Origins of Structural Flexibility in Protein-Based Supramolecular Polymers Revealed by DEER Spectroscopy.,Tavenor NA, Silva KI, Saxena S, Horne WS J Phys Chem B. 2014 Jul 24. PMID:25060334<ref>PMID:25060334</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: Saxena, S.]] | ||
| + | [[Category: Silva, K I.]] | ||
| + | [[Category: Tavenor, N A.]] | ||
| + | [[Category: Coiled coil]] | ||
Revision as of 02:21, 7 August 2014
GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 9
| |||||||||||
