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The cyclic AMP response element binding protein (CREB) contains a basic leucine zipper motif (bZIP) that forms a coiled coil structure upon dimerization and specific DNA binding. Although this state is well characterized, key features of CREB bZIP binding and folding are not well understood. We used single‐molecule Förster resonance energy transfer (smFRET) to probe conformations of CREB bZIP subdomains...
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