Kasper Planeta Kepp
Department of Chemistry, Technical University of Denmark
We are interested in understanding the natural evolution of proteins all the way from the individual amino acid changes, via the biophysical properties they give rise to, via the cell physiology, to the organism performance.
We call this concept "From Sequence to Survival". Our first case study has been the evolution of heme and myoglobin. We now understand the molecular evolution that has tuned heme to facilitate reversible spin crossover binding of oxygen, and how the protein in myoglobin optimizes the binding of oxygen.
We have also shown that oxygen storage and transport are too distinct functions manifesting differently in different mutants. Furthermore, while oxygen binding is similar in most mammalian myoglobins, its abundance differs by more than 10-fold.
We have shown that this correlates with protein stability and that molecular evolution of stability of highly expressed myoglobin is a key event in whales as they strived to become deep divers.