4hjd
From Proteopedia
(Difference between revisions)
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| - | + | ==GCN4pLI derivative with alpha/beta/acyclic-gamma amino acid substitution pattern== | |
| - | + | <StructureSection load='4hjd' size='340' side='right' caption='[[4hjd]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4hjd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HJD FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0W6:(4S)-4-AMINOPENTANOIC+ACID'>0W6</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=XCP:(1S,2S)-2-AMINOCYCLOPENTANECARBOXYLIC+ACID'>XCP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hjb|4hjb]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hjd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hjd RCSB], [http://www.ebi.ac.uk/pdbsum/4hjd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cyclic constraints have proven to be very effective for preorganizing beta-amino acid residues and thereby stabilizing beta- and alpha/beta-peptide helices, but little is known about possible preorganization effects among gamma residues. Here we assess and compare the impact of cyclic preorganization of beta and gamma residues in the context of a specific alpha/beta/gamma-peptide helix. The results show that beta residue preorganization is critical for helix stability but that gamma residue preorganization is less important. | ||
| - | + | Differential Impact of beta and gamma Residue Preorganization on alpha/beta/gamma-Peptide Helix Stability in Water.,Shin YH, Mortenson DE, Satyshur KA, Forest KT, Gellman SH J Am Chem Soc. 2013 May 23. PMID:23701135<ref>PMID:23701135</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Forest, K T | + | == References == |
| - | [[Category: Gellman, S H | + | <references/> |
| - | [[Category: Mortenson, D E | + | __TOC__ |
| - | [[Category: Satyshur, K A | + | </StructureSection> |
| - | [[Category: Shin, Y H | + | [[Category: Forest, K T]] |
| + | [[Category: Gellman, S H]] | ||
| + | [[Category: Mortenson, D E]] | ||
| + | [[Category: Satyshur, K A]] | ||
| + | [[Category: Shin, Y H]] | ||
[[Category: Alpha/beta/gamma amino acid]] | [[Category: Alpha/beta/gamma amino acid]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 11:59, 21 December 2014
GCN4pLI derivative with alpha/beta/acyclic-gamma amino acid substitution pattern
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