Enhancing the stability and folding rate of a repeat protein through the addition of consensus repeats.

ABSTRACT: Repeat proteins are constructed from a linear array of modular units, giving rise to an overall topology lacking long-range interactions. This suggests that stabilizing repeat modules based on consensus information might be added to a repeat protein domain, allowing it to be extended without altering its overall topology. Here we add consensus modules the ankyrin repeat domain from the Drosophila Notch receptor to investigate the structural tolerance to these modules, the relative thermodynamic stability of these hybrid proteins, and how alterations in the energy landscape influence folding kinetics. Insertions of consensus modules between repeats five and six of the Notch ankyrin domain have little effect on the far and near-UV CD spectra, indicating that neither secondary nor tertiary st

SUBMITTER: Tripp KW 

PROVIDER: S-EPMC1851695 | biostudies-literature | 2007 Jan

REPOSITORIES: biostudies-literature