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Mapping the Topography of a Protein Energy Landscape
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unpublished
Protein energy landscapes are highly complex, yet the vast majority of states within them tend to be invisible to experimentalists. Here, using site-directed mutagenesis and exploiting the simplicity of tandem-repeat protein structures, we delineate a network of these states and the routes between them. We show that our target, gankyrin, a 226residue 7-ankyrin-repeat protein, can access two alternative (un)folding pathways. We resolve intermediates as well as transition states, constituting a
doi:10.1021/jacs.5b07370.s001
fatcat:3rps27c2ofenndgvzc24dlbxhy