The effect of linker conformation on performance and stability of a two-domain lytic polysaccharide monooxygenase

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  1. Thank you for this amazing publication! I loved your paper! It's so cool how deeply you went to understand the function of a linker sequence using a variety of biophysical and computational techniques. Big kudos! I personally find it fascinating how a short amino acid sequence, that's technically not part of the core enzyme, could have such a profound impact on the main function of said protein! Specifically in your case, it seems the linker impacts catalytic activity as well as thermal stability of the enzyme. Also it seems that the linker may be impacting substrate binding. You speculate on this in the discussion but I was wondering if I could probe a little further. First, how much is known about the interaction of this enzyme with a complex substrate such as cellulose? For example, is this LPMO, or this class in general, a processive enzyme? Does the enzyme always remain bound to the substrate throughout catalysis? Or does it detach, and then re-attach? Second, is it known how LPMOs locate the scissile bond within the complex cellulose substrate? For example, do they attach at a random place on the substrate and then begin searching for the scissile bond (search in 2-D space)? Or do they search for the bond by attaching and detaching numerous times across the substrate (search in 3-D space)? Thank you so much for the cool paper! And thank you for your time!