4tl1: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 9==
<StructureSection load='4tl1' size='340' side='right' caption='[[4tl1]], [[Resolution|resolution]] 1.80&Aring;' 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.


The entry 4tl1 is ON HOLD  until Paper Publication
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>


Authors: Tavenor, N.A., Silva, K.I., Saxena, S., Horne, W.S.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 9
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Horne, W S.]]
[[Category: Saxena, S.]]
[[Category: Silva, K I.]]
[[Category: Tavenor, N A.]]
[[Category: Coiled coil]]
Retrieved from "https://proteopedia.org/4tl1"