Delta98Delta, a minimalist model of antiparallel beta-sheet proteins based on intestinal fatty acid binding protein.

ABSTRACT: The design of beta-barrels has always been a formidable challenge for de novo protein design. For instance, a persistent problem is posed by the intrinsic tendency to associate given by free edges. From the opposite standpoint provided by the redesign of natural motifs, we believe that the intestinal fatty acid binding protein (IFABP) framework allows room for intervention, giving rise to abridged forms from which lessons on beta-barrel architecture and stability could be learned. In this context, Delta98Delta (encompassing residues 29-126 of IFABP) emerges as a monomeric variant that folds properly, retaining functional activity, despite lacking extensive stretches involved in the closure of the beta-barrel. Spectroscopic probes (fluorescence and circular dichroism) support the existence

SUBMITTER: Curto LM 

PROVIDER: S-EPMC2762586 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature