Abstract
Repeat proteins greatly simplify the identification of the sequence determinants for protein folding cooperativity. We use the leucine rich repeat (LRR) domain of the tumor suppressor pp32 as a model. It is composed of five LRR with a capping domain on each of its termini. Previous pressure-dependent NMR experiments of cavity-containing mutants of pp32 revealed that the intermediates populated during pressure-induced unfolding depend upon the position of the cavity. In order to further characterize the nature of these intermediates, we carried out NMR relaxation experiments, relaxation dispersion (CPMG) and chemical exchange saturation transfer (CEST) experiments.
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