| pubmed-article:15653742 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C0008109 | lld:lifeskim |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C0007641 | lld:lifeskim |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C0205173 | lld:lifeskim |
| pubmed-article:15653742 | lifeskim:mentions | umls-concept:C0443220 | lld:lifeskim |
| pubmed-article:15653742 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15653742 | pubmed:dateCreated | 2005-3-28 | lld:pubmed |
| pubmed-article:15653742 | pubmed:abstractText | The structural properties of the linker peptide connecting the cellulose-binding module to the catalytic module in bimodular cellulases have been investigated by small-angle x-ray scattering. Since the linker and the cellulose-binding module are relatively small and cannot be readily detected separately, the conformation of the linker was studied by means of an artificial fusion protein, Cel6BA, in which an 88-residue linker connects the large catalytic modules of the cellulases Cel6A and Cel6B from Humicola insolens. Our data showed that Cel6BA is very elongated with a maximum dimension of 178 A, but could not be described by a single conformation. Modeling of a series of Cel6BA conformers with interdomain separations ranging between 10 A and 130 A showed that good Guinier and P(r) profile fits were obtained by a weighted average of the scattering curves of all the models where the linker follows a nonrandom distribution, with a preference for the more compact conformers. These structural properties are likely to be essential for the function of the linker as a molecular spring between the two functional modules. Small-angle x-ray scattering therefore provides a unique tool to quantitatively analyze the conformational disorder typical of proteins described as natively unfolded. | lld:pubmed |
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| pubmed-article:15653742 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15653742 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15653742 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15653742 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15653742 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:SchüleinMarti... | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:PerkinsStephe... | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:FrandsenTorbe... | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:EatonJulian... | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:HenrissatBern... | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:CzjzekMirjamM | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:PaninePierreP | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:von... | lld:pubmed |
| pubmed-article:15653742 | pubmed:author | pubmed-author:Receveur-Bréc... | lld:pubmed |
| pubmed-article:15653742 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15653742 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:15653742 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15653742 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15653742 | pubmed:pagination | 2823-32 | lld:pubmed |
| pubmed-article:15653742 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
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| pubmed-article:15653742 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15653742 | pubmed:articleTitle | Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase. | lld:pubmed |
| pubmed-article:15653742 | pubmed:affiliation | Novozymes A/S, Bagsvaerd, Denmark. | lld:pubmed |
| pubmed-article:15653742 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15653742 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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