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Biological Chemistry: Metal transport by proteins

While DNA contains the genetic information, a large number of different proteins are the ‘workhorses’ in living organisms executing the orders given through the DNA code. In order to function, most proteins (synthesised as long polypeptide chains) must fold into compact globular structures such that chemical groups are placed at the right positions for each protein’s specific function. In addition to folding, one third of all proteins need to bind metal ions to acquire the right properties. For example, essential proteins in respiration and photosynthesis only function with strategically-coordinated metal centers. Despite their fundamental importance, most free metals are toxic to living organisms. To overcome this paradox, living systems have developed elaborate metal-transport systems that appear to involve unique proteins for each metal.

In this project, the first goal is to design a plan to extend already successful in vitro biophysical research on copper transport proteins to (1) zinc and manganese transport proteins, for which less is known, and to (2) in vivo conditions exploring diseases related to problems with metal transport. In the second goal of the project, it will be investigated how life science, in general, and protein folding, in particular, can be brought into the General Chemistry curriculum to make the course timely and inspiring to undergraduate students. Interactions with local researchers in South Africa will provide input to the project.


Fellows involved in this project


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Is any information on this page incorrect or outdated? Please notify Ms. Nel-Mari Loock at [email protected].