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 15N-1H high-pressure HSQC experiments revealed that intermediates are populated in the folding of pp32, and in several cavity-containing variants. In order to obtain more information about these intermediates, in particular about the core packing, we collected 13C-1H HSQC spectra as a function of pressure on three cavity-containing variants of pp32, one in the N-terminus (I7A), one in the C-terminus (L139A) and one in the central core (L60A).
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