Abstract
Conformational changes of bovine α-lactalbumin induced by adsorption on a hydrophobic interface are studied by fluorescence and circular dichroism spectroscopy. Adsorption of bovine α-lactalbumin on hydrophobic polystyrene nanospheres induces a non-native state of the protein, which is characterized by preserved secondary structure, lost tertiary structure, and release of calcium. This partially denatured state therefore resembles a molten globule state, which is an intermediate in the folding of bovine α-lactalbumin. Stopped-flow fluorescence spectroscopy reveals two kinetic phases during adsorption with rate constants k
Original language | English |
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Pages (from-to) | 10922-10930 |
Journal | Journal of Biological Chemistry |
Volume | 277 |
DOIs | |
Publication status | Published - 2002 |