The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.

ABSTRACT: Intestinal fatty acid-binding protein (I-FABP) has a clam-shaped structure that may serve as a scaffold for the design of artificial enzymes and drug carriers. In an attempt to optimize the scaffold for increased access to the interior-binding cavity, several helix-less variants of I-FABP have been engineered. The solution-state NMR structure of the first generation helix-less variant, known as Delta17-SG, revealed a larger-than-expected and structurally ill-defined loop flanking the deletion site. We hypothesized that the presence of this loop, on balance, was energetically unfavorable for the stability of the protein. The structure exhibited no favorable pairwise or nonpolar interactions in the loop that could offset the loss of configurational entropy associated with the folding of this

SUBMITTER: Ogbay B 

PROVIDER: S-EPMC2286757 | biostudies-literature | 2004 May

REPOSITORIES: biostudies-literature