2MN4
NMR solution structure of a computational designed protein based on structure template 1cy5
Summary for 2MN4
| Entry DOI | 10.2210/pdb2mn4/pdb |
| Related | 2MLB |
| NMR Information | BMRB: 19879 |
| Descriptor | Computational designed protein based on structure template 1cy5 (1 entity in total) |
| Functional Keywords | protein design, statistical energy function, alpha-helical greek, protein evolution, de novo protein |
| Biological source | synthetic |
| Total number of polymer chains | 1 |
| Total formula weight | 12403.27 |
| Authors | |
| Primary citation | Xiong, P.,Wang, M.,Zhou, X.,Zhang, T.,Zhang, J.,Chen, Q.,Liu, H. Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldability Nat Commun, 5:5330-5330, 2014 Cited by PubMed Abstract: 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. PubMed: 25345468DOI: 10.1038/ncomms6330 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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