| pubmed-article:1069263 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1069263 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:1069263 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
| pubmed-article:1069263 | lifeskim:mentions | umls-concept:C2698172 | lld:lifeskim |
| pubmed-article:1069263 | lifeskim:mentions | umls-concept:C1708533 | lld:lifeskim |
| pubmed-article:1069263 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:1069263 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:1069263 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:1069263 | pubmed:dateCreated | 1977-1-29 | lld:pubmed |
| pubmed-article:1069263 | pubmed:abstractText | We calculate the surface area buried in subunit interfaces of human deoxyhemoglobin and of horse methemoglobin. A larger surface area is buried in deoxy- than in methemoglobin as a result of tertiary and quaternary structure changes. In both molecules the dimer-dimer interface is closepacked. This implies that hydrophobicity stabilizes the deoxystructure, the free energy spent in keeping the subunits in a low-affinity conformation being compensated by hydrophobic free energy due to the smaller surface area accessible to solvent. | lld:pubmed |
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| pubmed-article:1069263 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1069263 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1069263 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1069263 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1069263 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1069263 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1069263 | pubmed:author | pubmed-author:ChothiaCC | lld:pubmed |
| pubmed-article:1069263 | pubmed:author | pubmed-author:JaninJJ | lld:pubmed |
| pubmed-article:1069263 | pubmed:author | pubmed-author:WodakSS | lld:pubmed |
| pubmed-article:1069263 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1069263 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:1069263 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1069263 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1069263 | pubmed:pagination | 3793-7 | lld:pubmed |
| pubmed-article:1069263 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1069263 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:1069263 | pubmed:articleTitle | Role of subunit interfaces in the allosteric mechanism of hemoglobin. | lld:pubmed |
| pubmed-article:1069263 | pubmed:publicationType | Journal Article | lld:pubmed |
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