Probing Pressure Effects On Core Packing Of A Repeat Protein Using 13c Nmr
BIOPHYSICAL JOURNAL(2019)
摘要
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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