View source for 2ldj


==1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid==
<StructureSection load='2ldj' size='340' side='right'caption='[[2ldj]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ldj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGN:D-GLUTAMINE'>DGN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ldj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldj OCA], [https://pdbe.org/2ldj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldj RCSB], [https://www.ebi.ac.uk/pdbsum/2ldj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldj ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Judicious incorporation of d-amino acids in engineered proteins confers many advantages such as preventing degradation by endogenous proteases and promoting novel structures and functions not accessible to homochiral polypeptides. Glycine to d-alanine substitutions at the carboxy termini can stabilize alpha-helices by reducing conformational entropy. Beyond alanine, we propose additional side chain effects on the degree of stabilization conferred by d-amino acid substitutions. A detailed, molecular understanding of backbone and side chain interactions is important for developing rational, broadly applicable strategies in using d-amino acids to increase protein thermostability. Insight from structural bioinformatics combined with computational protein design can successfully guide the selection of stabilizing d-amino acid mutations. Substituting a key glycine in the Trp-cage miniprotein with d-Gln dramatically stabilizes the fold without altering the protein backbone. Stabilities of individual substitutions can be understood in terms of the balance of intramolecular forces both at the alpha-helix C-terminus and throughout the protein.

Computational Design of Thermostabilizing d-Amino Acid Substitutions.,Rodriguez-Granillo A, Annavarapu S, Zhang L, Koder RL, Nanda V J Am Chem Soc. 2011 Nov 23;133(46):18750-9. Epub 2011 Oct 27. PMID:21978298<ref>PMID:21978298</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ldj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Annavarapu S]]
[[Category: Granillo AR]]
[[Category: Koder R]]
[[Category: Nanda V]]
[[Category: Zhang L]]