2mlb

NMR solution structure of a computational designed protein based on template of human erythrocytic ubiquitin

spinqualitylabelsall models 2mlb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mlb is a 1 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The de novo design of amino acid sequences to fold into desired structures is a way to reach a more thorough understanding of how amino acid sequences encode protein structures and to supply methods for protein engineering. Notwithstanding significant breakthroughs, there are noteworthy limitations in current computational protein design. To overcome them needs computational models to complement current ones and experimental tools to provide extensive feedbacks to theory. Here we develop a comprehensive statistical energy function for protein design with a new general strategy and verify that it can complement and rival current well-established models. We establish that an experimental approach can be used to efficiently assess or improve the foldability of designed proteins. We report four de novo proteins for different targets, all experimentally verified to be well-folded, solved solution structures for two being in excellent agreement with respective design targets. Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldability.,Xiong P, Wang M, Zhou X, Zhang T, Zhang J, Chen Q, Liu H Nat Commun. 2014 Oct 27;5:5330. doi: 10.1038/ncomms6330. PMID:25345468 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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