pubmed-article:17394655 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17394655 | lifeskim:mentions | umls-concept:C0024501 | lld:lifeskim |
pubmed-article:17394655 | lifeskim:mentions | umls-concept:C0597570 | lld:lifeskim |
pubmed-article:17394655 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:17394655 | lifeskim:mentions | umls-concept:C0037628 | lld:lifeskim |
pubmed-article:17394655 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:17394655 | pubmed:dateCreated | 2007-4-13 | lld:pubmed |
pubmed-article:17394655 | pubmed:abstractText | The database of protein structures contains representatives from organisms with a range of growth temperatures. Various properties have been studied in a search for the molecular basis of protein adaptation to higher growth temperature. Charged groups have emerged as key distinguishing factors for proteins from thermophiles and mesophiles. | lld:pubmed |
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pubmed-article:17394655 | pubmed:language | eng | lld:pubmed |
pubmed-article:17394655 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17394655 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17394655 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |