Matches in DBpedia 2014 for { ?s ?p HMGA1-GFP fusion proteins are highly dynamic in vivo , but in contrast also show nanomolar affinity to AT-rich DNA in vitro which might be explained due to the extensive post-transcriptional modifications in vivo. HMGA1 preferentially binds to the minor groove of AT-rich regions in double-stranded DNA using its AT-hooks. It has little secondary structure in solution but assumes distinct conformations when bound to substrates such as DNA or other proteins. HMGA1 proteins have high amounts of diverse post-tranlational modifications and are located mainly in the nucleus, especially in heterochromatin, but also in mitochondria and the cytoplasm.. }
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- HMGA1 summaryText "HMGA1-GFP fusion proteins are highly dynamic in vivo , but in contrast also show nanomolar affinity to AT-rich DNA in vitro which might be explained due to the extensive post-transcriptional modifications in vivo. HMGA1 preferentially binds to the minor groove of AT-rich regions in double-stranded DNA using its AT-hooks. It has little secondary structure in solution but assumes distinct conformations when bound to substrates such as DNA or other proteins. HMGA1 proteins have high amounts of diverse post-tranlational modifications and are located mainly in the nucleus, especially in heterochromatin, but also in mitochondria and the cytoplasm.".