Article
Biophysical characterisation of the small ankyrin repeat protein myotrophin.
Journal of molecular biology - 26 Jan 2007
Lowe Alan R, Itzhaki Laura S
Abstract excerpt
The 118 residue protein myotrophin is composed of four ankyrin repeats that stack linearly to form an elongated, predominantly alpha-helical structure. The protein folds via a two-state mechanism at equilibrium. The free energy change of unfolding in water (DeltaG(U-N)(H(2)O)) is 5.8 kcal.mol(-1). The chevron plot reveals that the folding reaction has a broad energy barrier and that it conforms to a two-state...
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