A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins.

ABSTRACT: Partially folded proteins, characterized as exhibiting secondary structure elements with loose or absent tertiary contacts, represent important intermediates in both physiological protein folding and pathological protein misfolding. To aid in the characterization of the structural state(s) of such proteins, a novel structure calculation scheme is presented that combines structural restraints derived from pulsed EPR and NMR spectroscopy. The methodology is established for the protein alpha-synuclein (alphaS), which exhibits characteristics of a partially folded protein when bound to a micelle of the detergent sodium lauroyl sarcosinate (SLAS). By combining 18 EPR-derived interelectron spin label distance distributions with NMR-based secondary structure definitions and bond vector restraints

SUBMITTER: Rao JN 

PROVIDER: S-EPMC2903201 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature