Insights into the Structure of Invisible Conformations of Large Methyl Group Labeled Molecular Machines from High Pressure NMR

URN to cite this document:: urn:nbn:de:bvb:355-epub-543905
DOI to cite this document:: 10.5283/epub.54390

Krempl, Christina ; Wurm, Jan Philip

; Beck Erlach, Markus ; Kremer, Werner

; Sprangers, Remco

License: Creative Commons Attribution Non-commercial 4.0
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Date of publication of this fulltext: 21 Jun 2023 08:25

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Abstract

Most proteins are highly flexible and can adopt conformations that deviate from the energetically most favorable ground state. Structural information on these lowly populated, alternative conformations is often lacking, despite the functional importance of these states. Here, we study the pathway by which the Dcp1:Dcp2 mRNA decapping complex exchanges between an autoinhibited closed and an open ...