| pubmed-article:7607330 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C0041078 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C0427716 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C1304757 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C2698172 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C1708533 | lld:lifeskim |
| pubmed-article:7607330 | lifeskim:mentions | umls-concept:C1550572 | lld:lifeskim |
| pubmed-article:7607330 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7607330 | pubmed:dateCreated | 1995-8-17 | lld:pubmed |
| pubmed-article:7607330 | pubmed:abstractText | Wild-type trypanosomal triosephosphate isomerase (wtTIM) is a very tight dimer. The interface residue His-47 of wtTIM has been mutated into an asparagine. Ultracentrifugation data show that this variant (H47N) only dimerises at protein concentrations above 3 mg/ml. H47N has been characterised at a protein concentration where it is predominantly a monomer. Circular dichroism measurements in the near-UV and far-UV show that this monomer is a compactly folded protein with secondary structure similar as in wtTIM. The thermal stability of the monomeric H47N is decreased compared to wtTIM: temperature gradient gel electrophoresis (TGGE) measurements give Tm-values of 41 degrees C for wtTIM, whereas the Tm-value for the monomeric form of H47N is approximately 7 degrees C lower. | lld:pubmed |
| pubmed-article:7607330 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7607330 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7607330 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7607330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7607330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7607330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7607330 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7607330 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7607330 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:JaenickeRR | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:WierengaR KRK | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:CallensMM | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:ZeelenJ PJP | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:BorchertT VTV | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:SchliebsWW | lld:pubmed |
| pubmed-article:7607330 | pubmed:author | pubmed-author:MinkaSS | lld:pubmed |
| pubmed-article:7607330 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7607330 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:7607330 | pubmed:volume | 367 | lld:pubmed |
| pubmed-article:7607330 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7607330 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7607330 | pubmed:pagination | 315-8 | lld:pubmed |
| pubmed-article:7607330 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:meshHeading | pubmed-meshheading:7607330-... | lld:pubmed |
| pubmed-article:7607330 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7607330 | pubmed:articleTitle | An interface point-mutation variant of triosephosphate isomerase is compactly folded and monomeric at low protein concentrations. | lld:pubmed |
| pubmed-article:7607330 | pubmed:affiliation | EMBL, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:7607330 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7607330 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7607330 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7607330 | lld:pubmed |
