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pubmed-article:1782805pubmed:abstractTextCircular dichroism and fluorescence measurements showed a reduced conformational order in proteins of a normal human lens when they were incubated in vitro with melittin, a bee venom peptide. Since melittin is also known to react with lipids to induce a breakdown of vesicular structure, the observed denaturation of water-soluble proteins of a human lens that developed a cataract due to multiple bee stings may be accounted for by the effects of melittin to some extent. The melittin-induced decrease of conformational order, as observed in our in-vitro studies could thus be of physiological significance.lld:pubmed
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pubmed-article:1782805pubmed:authorpubmed-author:ChakrabartiBBlld:pubmed
pubmed-article:1782805pubmed:authorpubmed-author:GhoshS KSKlld:pubmed
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pubmed-article:1782805pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:1782805pubmed:articleTitleMelittin-induced conformational changes in human lens protein.lld:pubmed
pubmed-article:1782805pubmed:affiliationDivision of Crystallography and Molecular Biology, Saha Institute of Nuclear Physics, Calcutta, India.lld:pubmed
pubmed-article:1782805pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1782805pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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