| pubmed-article:8402272 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C0001898 | lld:lifeskim |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C0022192 | lld:lifeskim |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C0314672 | lld:lifeskim |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C0037628 | lld:lifeskim |
| pubmed-article:8402272 | lifeskim:mentions | umls-concept:C1979845 | lld:lifeskim |
| pubmed-article:8402272 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8402272 | pubmed:dateCreated | 1993-11-24 | lld:pubmed |
| pubmed-article:8402272 | pubmed:abstractText | The Hb S (beta 6 Glu-->Val) fiber is formed by the packing of double strands which constitute the basic unit of the deoxyHb S polymer. The specific interaction responsible for the stabilization of the double strand involves the mutated beta 6 Val side chain (lateral contact). Recombinant Hb beta 6 Glu-->Ala and the double mutant beta 6 Glu-->Ala, 23 Val-->Ile exhibit a decreased solubility compared to Hb A. While the Hb beta 6 Ala does not polymerize, the association of the beta 23 Val-->Ile mutation at the axial contact allows the double mutant to polymerize. These results show that: (1) the hydrophobic interactions between donor and acceptor sites depend on both the hydrophobicity and the stereospecificity of the amino acid side chain at the beta 6 position; (2) increasing the hydrophobic interactions at the axial contact (connecting molecules along the same strand) result in an increased stability of the lateral contact between filaments. | lld:pubmed |
| pubmed-article:8402272 | pubmed:language | fre | lld:pubmed |
| pubmed-article:8402272 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8402272 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8402272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8402272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8402272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8402272 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8402272 | pubmed:issn | 0764-4469 | lld:pubmed |
| pubmed-article:8402272 | pubmed:author | pubmed-author:PoyartCC | lld:pubmed |
| pubmed-article:8402272 | pubmed:author | pubmed-author:PagnierJJ | lld:pubmed |
| pubmed-article:8402272 | pubmed:author | pubmed-author:EdelsteinS... | lld:pubmed |
| pubmed-article:8402272 | pubmed:author | pubmed-author:BaudinVV | lld:pubmed |
| pubmed-article:8402272 | pubmed:author | pubmed-author:BihoreauM TMT | lld:pubmed |
| pubmed-article:8402272 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8402272 | pubmed:volume | 316 | lld:pubmed |
| pubmed-article:8402272 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8402272 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8402272 | pubmed:pagination | 431-6 | lld:pubmed |
| pubmed-article:8402272 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8402272 | pubmed:meshHeading | pubmed-meshheading:8402272-... | lld:pubmed |
| pubmed-article:8402272 | pubmed:meshHeading | pubmed-meshheading:8402272-... | lld:pubmed |
| pubmed-article:8402272 | pubmed:meshHeading | pubmed-meshheading:8402272-... | lld:pubmed |
| pubmed-article:8402272 | pubmed:meshHeading | pubmed-meshheading:8402272-... | lld:pubmed |
| pubmed-article:8402272 | pubmed:meshHeading | pubmed-meshheading:8402272-... | lld:pubmed |
| pubmed-article:8402272 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8402272 | pubmed:articleTitle | [Polymerization and solubility of recombinant hemoglobins alpha 2 beta 2 6 Glu-->Ala (Hb Makassar) and alpha 2 beta 2 6 Glu-->Ala, 23 Val-->Ile]. | lld:pubmed |
| pubmed-article:8402272 | pubmed:affiliation | INSERM U299, Hôpital de Bicêtre, Le Kremlin-Bicêtre, France. | lld:pubmed |
| pubmed-article:8402272 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8402272 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8402272 | pubmed:publicationType | English Abstract | lld:pubmed |
| pubmed-article:8402272 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
