| pubmed-article:19450485 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19450485 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:19450485 | lifeskim:mentions | umls-concept:C0019534 | lld:lifeskim |
| pubmed-article:19450485 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19450485 | lifeskim:mentions | umls-concept:C0152058 | lld:lifeskim |
| pubmed-article:19450485 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:19450485 | pubmed:dateCreated | 2009-5-19 | lld:pubmed |
| pubmed-article:19450485 | pubmed:abstractText | HMGA2 is a DNA minor-groove binding protein. We previously demonstrated that HMGA2 binds to AT-rich DNA with very high binding affinity where the binding of HMGA2 to poly(dA-dT)(2) is enthalpy-driven and to poly(dA)poly(dT) is entropy-driven. This is a typical example of enthalpy-entropy compensation. To further study enthalpy-entropy compensation of HMGA2, we used isothermal-titration-calorimetry to examine the interactions of HMGA2 with two AT-rich DNA hairpins: 5'-CCAAAAAAAAAAAAAAAGCCCCCGCTTTTTTTTTTTTTTTGG-3' (FL-AT-1) and 5'-CCATATATATATATATAGCCCCCGCTATATATATATATATGG-3' (FL-AT-2). Surprisingly, we observed an atypical isothermal-titration-calorimetry-binding curve at low-salt aqueous solutions whereby the apparent binding-enthalpy decreased dramatically as the titration approached the end. This unusual behavior can be attributed to the DNA-annealing coupled to the ligand DNA-binding and is eliminated by increasing the salt concentration to approximately 200 mM. At this condition, HMGA2 binding to FL-AT-1 is entropy-driven and to FL-AT-2 is enthalpy-driven. Interestingly, the DNA-binding free energies for HMGA2 binding to both hairpins are almost temperature independent; however, the enthalpy-entropy changes are dependent on temperature, which is another aspect of enthalpy-entropy compensation. The heat capacity change for HMGA2 binding to FL-AT-1 and FL-AT-2 are almost identical, indicating that the solvent displacement and charge-charge interaction in the coupled folding/binding processes for both binding reactions are similar. | lld:pubmed |
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| pubmed-article:19450485 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19450485 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19450485 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19450485 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19450485 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19450485 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19450485 | pubmed:month | May | lld:pubmed |
| pubmed-article:19450485 | pubmed:issn | 1542-0086 | lld:pubmed |
| pubmed-article:19450485 | pubmed:author | pubmed-author:LengFenfeiF | lld:pubmed |
| pubmed-article:19450485 | pubmed:author | pubmed-author:JoyntSuzanneS | lld:pubmed |
| pubmed-article:19450485 | pubmed:author | pubmed-author:MorilloVictor... | lld:pubmed |
| pubmed-article:19450485 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19450485 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:19450485 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:19450485 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19450485 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19450485 | pubmed:pagination | 4144-52 | lld:pubmed |
| pubmed-article:19450485 | pubmed:dateRevised | 2010-9-24 | lld:pubmed |
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| pubmed-article:19450485 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19450485 | pubmed:articleTitle | Binding the mammalian high mobility group protein AT-hook 2 to AT-rich deoxyoligonucleotides: enthalpy-entropy compensation. | lld:pubmed |
| pubmed-article:19450485 | pubmed:affiliation | Department of Chemistry & Biochemistry, Florida International University, Miami, Florida 33199, USA. | lld:pubmed |
| pubmed-article:19450485 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19450485 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19450485 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19450485 | lld:pubmed |
