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Na publikacji autorka Wolczko Marta podpisana jako Molenda Marta.
język:
angielski
język czasopisma:
angielski
abstrakt w j. angielskim:
Ovine
b
-lactoglobulin has been isolated from whey frac-
tion of sheep milk and crystallized. The high-resolution
structures of two crystal forms (triclinic and trigonal)
obtained at pH 7.0 have been determined revealing that
ovine protein, similarly to its bovine analog, is dimeric.
Access to the binding site located in the eight-stranded
antiparallel
b
-barrel in both structures is blocked by the
EF loop that has been found in closed conformation. Sim-
ilarly to bovine lactoglobulin (BLG), conformation of the
EF loop is stabilized by hydrogen bond between Glu89
and Ser116 indicating that Tanford transition might
occur with the same mechanism. The substitution at six
positions in relation to the most abundant isoform B of
BLG also affects the distribution of electrostatic potentials
and the total charge.