Polyhedric features of cysteine: from protein functionalization to copper-binding
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Date
2015-03-30Author
Cattani, Giada
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Abstract
This thesis comprises two main projects which are about the
cysteine chemistry involved in protein functionalization and copperbinding.
Plastocyanin functionalization via cysteine has been used to
produce a conjugate for the aim of obtaining structural information of a
self-assembled state directed by the conjugation. This aim was achieved
with a PEGylated Plastocyanin by using NMR spectroscopy and X-ray
crystallography. The first crystal structure of a PEGylated protein has
been solved at a resolution of 4.2 Å. The electron density of the PEG
chain is not visible suggesting a highly disordered structure, but the
crystal packing is remarkable: a right-handed antiparallel double-helical
assembly was observed.
In biological systems cysteine can be coordinated to copper, an
essential trace element which is associated with neurodegenerative
disorders and therefore its trafficking is regulated in cells. The
preliminary NMR study of a novel cysteine rich copper-binding protein
found by the group of Prof. Dennison in Newcastle University (UK) is
presented. 15N-, 13C15N- and 15N-selective amino acid labelled protein
samples were produced to assign the backbone resonances and to study
the binding of copper.