TY - JOUR
T1 - Kinetic and structural characterisation of adsorption induced unfolding of bovine & alpha;-lactalbumin
AU - Engel, M.F.M.
AU - Van Mierlo, C.P.M.
AU - Visser, A.J.W.G.
PY - 2002
Y1 - 2002
N2 - 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
AB - 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
UR - https://www.scopus.com/pages/publications/0037192769
UR - https://www.scopus.com/inward/citedby.url?scp=0037192769&partnerID=8YFLogxK
U2 - 10.1074/jbc.M106005200
DO - 10.1074/jbc.M106005200
M3 - Article
SN - 0021-9258
VL - 277
SP - 10922
EP - 10930
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
ER -
