BibTeX
@MISC{Roder08availableonline,
author = {Heinrich Roder},
title = {Available online},
year = {2008}
}
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Abstract
doi:10.1016/j.jmb.2008.08.025 Available online at wwwIntroduction Metalloproteins often depend on their cofactor not only for function but also for efficient folding and stabilization of their native structure. For example, in the absence of heme, myoglobin folds into a margin-ally stable state lacking some of the native α-helices and tertiary interactions,1 and cytochrome b562 assumes a dynamic molten-globule-like confor-mation.2 An even more extreme case is cytochrome c (cyt c), which is initially synthesized as a largely disordered apoprotein3,4 and folds into a stable globular structure only after covalent attachment of
