pubmed-article:17289254 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0014653 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0041942 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0598629 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0994894 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C1706366 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0439237 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0120447 | lld:lifeskim |
pubmed-article:17289254 | lifeskim:mentions | umls-concept:C0005249 | lld:lifeskim |
pubmed-article:17289254 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:17289254 | pubmed:dateCreated | 2007-3-26 | lld:pubmed |
pubmed-article:17289254 | pubmed:abstractText | We have carried out guanidinium chloride (GdmCl) and urea denaturations of bovine beta-lactoglobulin A (beta-lgA) at pH 2.0 and 25 degrees C, using far-UV and near-UV circular dichroism, near-UV absorption and tryptophan fluorescence spectroscopies. The stable intermediate state that occurs during GdmCl denaturation has been characterized by the far- and near-UV circular dichroism, tryptophan difference absorption, tryptophan fluorescence and 8-anilino-1-naphthalene sulphonic acid binding measurements. Following conclusions have been reached. (a) Urea-induced denaturation is not a two-state process. (b) GdmCl-induced denaturation is composed of two distinct two-state processes. (c) alpha-Helical content, burial of tryptophan residues and burial of hydrophobic surface area are more in the GdmCl-induced stable intermediate than those originally present in the native protein. | lld:pubmed |
pubmed-article:17289254 | pubmed:language | eng | lld:pubmed |
pubmed-article:17289254 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17289254 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17289254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17289254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17289254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17289254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17289254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17289254 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17289254 | pubmed:month | May | lld:pubmed |
pubmed-article:17289254 | pubmed:issn | 0301-4622 | lld:pubmed |
pubmed-article:17289254 | pubmed:author | pubmed-author:Moosavi-Movah... | lld:pubmed |
pubmed-article:17289254 | pubmed:author | pubmed-author:AhmadFaizanF | lld:pubmed |
pubmed-article:17289254 | pubmed:author | pubmed-author:IslamAsimulA | lld:pubmed |
pubmed-article:17289254 | pubmed:author | pubmed-author:AnjumFarahF | lld:pubmed |
pubmed-article:17289254 | pubmed:author | pubmed-author:DarTanveer... | lld:pubmed |
pubmed-article:17289254 | pubmed:author | pubmed-author:SinghLaishram... | lld:pubmed |
pubmed-article:17289254 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17289254 | pubmed:volume | 127 | lld:pubmed |
pubmed-article:17289254 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17289254 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17289254 | pubmed:pagination | 140-8 | lld:pubmed |
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pubmed-article:17289254 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17289254 | pubmed:articleTitle | Guanidinium chloride and urea denaturations of beta-lactoglobulin A at pH 2.0 and 25 degrees C: the equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches). | lld:pubmed |
pubmed-article:17289254 | pubmed:affiliation | Department of Biosciences, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi-110 025, India. | lld:pubmed |
pubmed-article:17289254 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17289254 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |