NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system.

ABSTRACT: In patients with dialysis-related amyloidosis, beta2-microglobulin (beta2-m) is a major structural component of amyloid fibrils. It has been suggested that the partial unfolding of beta2-m is a prerequisite to the formation of amyloid fibrils, and that the folding intermediate trapped by the non-native trans-Pro32 isomer leads to the formation of amyloid fibrils. Although clarifying the structure of this refolding intermediate by high resolution NMR spectroscopy is important, this has been made difficult by the limited lifetime of the intermediate. Here, we studied the structure of the refolding intermediate using a combination of amino acid selective labeling with wheat germ cell-free protein synthesis and NMR techniques. The HSQC spectra of beta2-ms labeled selectively at either phenylal

SUBMITTER: Kameda A 

PROVIDER: S-EPMC2776947 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature