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- W3133781888 endingPage "1116" @default.
- W3133781888 startingPage "1085" @default.
- W3133781888 abstract "Metal ions play many critical roles in biology, as structural and catalytic cofactors, and as cell regulatory and signalling elements. The metal–protein affinity, expressed conveniently by the metal dissociation constant, KD, describes the thermodynamic strength of a metal–protein interaction and is a key parameter that can be used, for example, to understand how proteins may acquire metals in a cell and to identify dynamic elements (e.g. cofactor binding, changing metal availabilities) which regulate protein metalation in vivo. Here, we outline the fundamental principles and practical considerations that are key to the reliable quantification of metal–protein affinities. We review a selection of spectroscopic probes which can be used to determine protein affinities for essential biological transition metals (including Mn(II), Fe(II), Co(II), Ni(II), Cu(I), Cu(II) and Zn(II)) and, using selected examples, demonstrate how rational probe selection combined with prudent experimental design can be applied to determine accurate KD values." @default.
- W3133781888 created "2021-03-15" @default.
- W3133781888 creator A5010219322 @default.
- W3133781888 creator A5029281644 @default.
- W3133781888 date "2021-03-10" @default.
- W3133781888 modified "2023-10-10" @default.
- W3133781888 title "Principles and practice of determining metal–protein affinities" @default.
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