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Metal ions and protein folding: conformational and functional interplay
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Metal ions are cofactors in about 30% of all proteins, where they fulfill
catalytical and structural roles. Due to their unique chemistry and
coordination properties they effectively expand the intrinsic polypeptide
properties (by participating in catalysis or electron transfer reactions),
stabilize protein conformations (like in zinc fingers) and mediate signal
transduction (by promoting functionally relevant protein conformational
changes). However, metal ions can also exert have deleterious effects in
living systems by incorporating in non-native binding sites, promoting
aberrant protein aggregation or mediating redox cycling with generation of
reactive oxygen and nitrogen species. For this reason, the characterization of
the roles of metal ions as modulators of protein conformation and stability
provides fundamental knowledge on protein folding properties and is
instrumental in establishing the molecular basis of disease. In this thesis we
have analyzed protein folding processes using model protein systems
incorporating covalently bound metal cofactors – iron-sulfur (FeS) proteins –
or where metal ion binding is reversible and associated conformational
readjustments – the S100 proteins.(...)
Descrição
Dissertation presented to obtain a PhD degree in Biochemistry at Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa
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Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa