Directional copper trafficking: In vitro and in vivo studies of metal binding and transfer

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A protein is a biological polymer with a complex three-dimensional structure. Many proteins bind metal ions which are usually essential for both structure and function even though the metals constitute typically less than 0.5 % of the total mass of the molecule (approximately one third of all proteins contain metals and these molecules are called metalloproteins). Metal ions have to be incorporated into the correct proteins within cells, and systems (networks of proteins) are emerging via which this is achieved. These regulatory networks of proteins also prevent the potentially damaging effects of the uncontrolled reactivity of metal ions and when these systems are impaired various diseases can result. The proposed studies aim to investigate the proteins which are responsible for ensuring that copper is supplied to the correct destination in a relatively simple model organism. Metal affinities of all of the proteins involved will be determined as will their ability to transfer copper. The effects of designed alterations to the protein structure on metal binding and transfer, protein interactions as well as the influence on physiological activity in the model organism will all be assessed. A detailed appreciation of the factors regulating this important biological process will be obtained.