This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2ldj
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid== | ==1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid== | ||
| - | <StructureSection load='2ldj' size='340' side='right' caption='[[2ldj | + | <StructureSection load='2ldj' size='340' side='right'caption='[[2ldj]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2ldj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDJ OCA]. <br> | + | <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> |
| - | <b> | + | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
| Line 9: | Line 13: | ||
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> | 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2ldj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Annavarapu | + | [[Category: Large Structures]] |
| - | [[Category: Granillo | + | [[Category: Annavarapu S]] |
| - | [[Category: Koder | + | [[Category: Granillo AR]] |
| - | [[Category: Nanda | + | [[Category: Koder R]] |
| - | [[Category: Zhang | + | [[Category: Nanda V]] |
| - | + | [[Category: Zhang L]] | |
| - | + | ||
| - | + | ||
Current revision
1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid
| |||||||||||
