2p6j
From Proteopedia
(New page: 200px<br /><applet load="2p6j" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p6j" /> '''Full-sequence computational design and solut...) |
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==Overview== | ==Overview== | ||
| - | Computational protein design procedures were applied to the redesign of | + | Computational protein design procedures were applied to the redesign of the entire sequence of a 51 amino acid residue protein, Drosophila melanogaster engrailed homeodomain. Various sequence optimization algorithms were compared and two resulting designed sequences were experimentally evaluated. The two sequences differ by 11 mutations and share 22% and 24% sequence identity with the wild-type protein. Both computationally designed proteins were considerably more stable than the naturally occurring protein, with midpoints of thermal denaturation greater than 99 degrees C. The solution structure was determined for one of the two sequences using multidimensional heteronuclear NMR spectroscopy, and the structure was found to closely match the original design template scaffold. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Full-sequence | + | Full-sequence computational design and solution structure of a thermostable protein variant., Shah PS, Hom GK, Ross SA, Lassila JK, Crowhurst KA, Mayo SL, J Mol Biol. 2007 Sep 7;372(1):1-6. Epub 2007 Jun 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17628593 17628593] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Unidentified]] | [[Category: Unidentified]] | ||
| - | [[Category: Crowhurst, K | + | [[Category: Crowhurst, K A.]] |
| - | [[Category: Hom, G | + | [[Category: Hom, G K.]] |
| - | [[Category: Lassila, J | + | [[Category: Lassila, J K.]] |
| - | [[Category: Mayo, S | + | [[Category: Mayo, S L.]] |
| - | [[Category: Ross, S | + | [[Category: Ross, S A.]] |
| - | [[Category: Shah, P | + | [[Category: Shah, P S.]] |
[[Category: computational protein design]] | [[Category: computational protein design]] | ||
[[Category: de novo protein]] | [[Category: de novo protein]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:26:26 2008'' |
Revision as of 16:26, 21 February 2008
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Full-sequence computational design and solution structure of a thermostable protein variant
Overview
Computational protein design procedures were applied to the redesign of the entire sequence of a 51 amino acid residue protein, Drosophila melanogaster engrailed homeodomain. Various sequence optimization algorithms were compared and two resulting designed sequences were experimentally evaluated. The two sequences differ by 11 mutations and share 22% and 24% sequence identity with the wild-type protein. Both computationally designed proteins were considerably more stable than the naturally occurring protein, with midpoints of thermal denaturation greater than 99 degrees C. The solution structure was determined for one of the two sequences using multidimensional heteronuclear NMR spectroscopy, and the structure was found to closely match the original design template scaffold.
About this Structure
2P6J is a Protein complex structure of sequences from Unidentified. Full crystallographic information is available from OCA.
Reference
Full-sequence computational design and solution structure of a thermostable protein variant., Shah PS, Hom GK, Ross SA, Lassila JK, Crowhurst KA, Mayo SL, J Mol Biol. 2007 Sep 7;372(1):1-6. Epub 2007 Jun 16. PMID:17628593
Page seeded by OCA on Thu Feb 21 18:26:26 2008
