rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1993-7-9
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1304906-1055377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1304906-2007116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1304906-2107612,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
236-44
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1304906-Animals,
pubmed-meshheading:1304906-Circular Dichroism,
pubmed-meshheading:1304906-Dose-Response Relationship, Drug,
pubmed-meshheading:1304906-Guanidine,
pubmed-meshheading:1304906-Guanidines,
pubmed-meshheading:1304906-Hydrogen-Ion Concentration,
pubmed-meshheading:1304906-Mice,
pubmed-meshheading:1304906-Nerve Growth Factors,
pubmed-meshheading:1304906-Protein Denaturation,
pubmed-meshheading:1304906-Protein Folding,
pubmed-meshheading:1304906-Spectrometry, Fluorescence,
pubmed-meshheading:1304906-Ultraviolet Rays,
pubmed-meshheading:1304906-Urea
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pubmed:year |
1992
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pubmed:articleTitle |
Equilibrium denaturation studies of mouse beta-nerve growth factor.
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pubmed:affiliation |
Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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