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rdf:type |
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lifeskim:mentions |
umls-concept:C0021027,
umls-concept:C0026832,
umls-concept:C0162610,
umls-concept:C0205360,
umls-concept:C0678594,
umls-concept:C1514562,
umls-concept:C1704319,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883220,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
1997-1-23
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pubmed:databankReference |
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/telokin,
http://linkedlifedata.com/resource/pubmed/chemical/unc-22 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
624-39
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8969309-Amino Acid Sequence,
pubmed-meshheading:8969309-Animals,
pubmed-meshheading:8969309-Caenorhabditis elegans,
pubmed-meshheading:8969309-Caenorhabditis elegans Proteins,
pubmed-meshheading:8969309-Calmodulin-Binding Proteins,
pubmed-meshheading:8969309-Helminth Proteins,
pubmed-meshheading:8969309-Immunoglobulins,
pubmed-meshheading:8969309-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8969309-Molecular Sequence Data,
pubmed-meshheading:8969309-Muscle Proteins,
pubmed-meshheading:8969309-Myosin-Light-Chain Kinase,
pubmed-meshheading:8969309-Peptide Fragments,
pubmed-meshheading:8969309-Peptides,
pubmed-meshheading:8969309-Protein Denaturation,
pubmed-meshheading:8969309-Protein Folding,
pubmed-meshheading:8969309-Protein Structure, Secondary,
pubmed-meshheading:8969309-Protein Structure, Tertiary,
pubmed-meshheading:8969309-Sequence Alignment
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pubmed:year |
1996
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pubmed:articleTitle |
Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans.
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pubmed:affiliation |
Centre for Protein Engineering, MRC Unit of Protein Folding and Design, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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