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- W188839635 abstract "This chapter discusses the localization of calcium and zinc binding sites. Proton NMR titration experiments with bovine and human apo-α lactalbumin suggest that the protein undergoes only minor rearrangement in its overall structure upon binding a variety of di- and tri valent metal ions. Titration with one equivalent of Ca2+ and lanthanides causes changes in some of the upfield shifted methyl resonances, very minor changes in the aromatic resonances and a marked upfield shift of the Met-90 resonance. The existence of separate binding sites for the Ca2+ and Zn2+ classes of metal ions. Because both Zn2+ and Ca2+ have an effect on the Met-90 residue it is likely that the Zn2+ binds relatively close to the Ca2+-site, in agreement with earlier fluorescence measurements which indicated a distance of 12 Å between the sites. Both sites can be occupied simultaneously, but the occupation of the Ca2+ site has a dominant effect on the protein conformation." @default.
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- W188839635 date "1987-01-01" @default.
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- W188839635 title "NMR STUDIES OF METAL ION BINDING TO α-LACTALBUMIN: LOCALIZATION OF CALCIUM AND ZINC BINDING SITES11sponsored by the Medical Research Council of Canada." @default.
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- W188839635 doi "https://doi.org/10.1016/b978-0-12-521040-9.50068-1" @default.
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