pubmed-article:1304906 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1304906 | lifeskim:mentions | umls-concept:C0014653 | lld:lifeskim |
pubmed-article:1304906 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:1304906 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:1304906 | lifeskim:mentions | umls-concept:C0027753 | lld:lifeskim |
pubmed-article:1304906 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:1304906 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:1304906 | pubmed:dateCreated | 1993-7-9 | lld:pubmed |
pubmed-article:1304906 | pubmed:abstractText | Equilibrium denaturation of dimeric mouse beta-nerve growth factor (beta-NGF) has been studied by monitoring changes in the protein's spectroscopic characteristics. Denaturation of beta-NGF in guanidine hydrochloride and urea resulted in an altered intrinsic fluorescence emission spectrum, fluorescence depolarization, and diminished negative circular dichroism. Native-like spectroscopic properties and specific biological activity are restored when denaturant is diluted from unfolded samples, demonstrating that this process is fully reversible. However, refolding of denatured beta-NGF is dependent on the three disulfide bonds present in the native protein and does not readily occur when the disulfide bonds are reduced. Graphical analysis and nonlinear least-squares fitting of beta-NGF denaturation data demonstrate that denaturation is dependent on the concentration of beta-NGF and is consistent with a two-state model involving native dimer and denatured monomer (N2 = 2D). The conformational stability of mouse beta-NGF calculated according to this model is 19.3 +/- 1.1 kcal/mol in 100 mM sodium phosphate at pH 7. Increasing the hydrogen ion concentration resulted in a 25% decrease in beta-NGF stability at pH 4 relative to pH 7. | lld:pubmed |
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pubmed-article:1304906 | pubmed:language | eng | lld:pubmed |
pubmed-article:1304906 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1304906 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1304906 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1304906 | pubmed:month | Feb | lld:pubmed |
pubmed-article:1304906 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:1304906 | pubmed:author | pubmed-author:NeetK EKE | lld:pubmed |
pubmed-article:1304906 | pubmed:author | pubmed-author:TimmD EDE | lld:pubmed |
pubmed-article:1304906 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1304906 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:1304906 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1304906 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1304906 | pubmed:pagination | 236-44 | lld:pubmed |
pubmed-article:1304906 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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pubmed-article:1304906 | pubmed:meshHeading | pubmed-meshheading:1304906-... | lld:pubmed |
pubmed-article:1304906 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1304906 | pubmed:articleTitle | Equilibrium denaturation studies of mouse beta-nerve growth factor. | lld:pubmed |
pubmed-article:1304906 | pubmed:affiliation | Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106. | lld:pubmed |
pubmed-article:1304906 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1304906 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1304906 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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