2ldj

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[[Image:2ldj.png|left|200px]]
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==1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid==
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<StructureSection load='2ldj' size='340' side='right' caption='[[2ldj]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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== Structural highlights ==
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[[2ldj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDJ OCA]. <br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_2ldj", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2ldj| PDB=2ldj | SCENE= }}
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===1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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__TOC__
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The line below this paragraph, {{ABSTRACT_PUBMED_21978298}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 21978298 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21978298}}
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==About this Structure==
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[[2ldj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDJ OCA].
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==Reference==
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<ref group="xtra">PMID:021978298</ref><references group="xtra"/>
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[[Category: Annavarapu, S.]]
[[Category: Annavarapu, S.]]
[[Category: Granillo, A R.]]
[[Category: Granillo, A R.]]

Revision as of 08:40, 30 April 2014

1H Chemical Shift Assignments and structure of Trp-Cage mini-protein with D-amino acid

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