Abstract
Abstract: Intrinsic fluorescence and NMR-spectroscopy demonstrate that heat treatment of the ricin carbohydrate binding subunit (RTB) leads to partial unfolding to an intermediate stable state with enhanced amino acid side chain mobility and a redistribution of surface charges. RTB continues to facilitate transmembrane translocation of the enzymatically active ricin subunit (RTA) although its lectin activity and ability to interact with RTA are dramaticaJiy reduced following this thermal modification. The proposal that RTB potentiates membrane translocation of the A-chain in this intermediate folded state is discussed.
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