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| pubmed-article:8969309 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
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| pubmed-article:8969309 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:8969309 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8969309 | pubmed:dateCreated | 1997-1-23 | lld:pubmed |
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| pubmed-article:8969309 | pubmed:abstractText | The NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the immunoglobulin superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant. | lld:pubmed |
| pubmed-article:8969309 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8969309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969309 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8969309 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8969309 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8969309 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:ChothiaCC | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:FongSS | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:ClarkeJJ | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:BenianG MGM | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:FreundS MSM | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:ProctorMM | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:BycroftMM | lld:pubmed |
| pubmed-article:8969309 | pubmed:author | pubmed-author:HamillS JSJ | lld:pubmed |
| pubmed-article:8969309 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8969309 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:8969309 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:8969309 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8969309 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8969309 | pubmed:pagination | 624-39 | lld:pubmed |
| pubmed-article:8969309 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8969309 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8969309 | pubmed:articleTitle | Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. | lld:pubmed |
| pubmed-article:8969309 | pubmed:affiliation | Centre for Protein Engineering, MRC Unit of Protein Folding and Design, Cambridge, UK. | lld:pubmed |
| pubmed-article:8969309 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8969309 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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