• appel@whiskers.bim.boats
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      1 year ago

      Thanks for the explanation, but I still don’t quite see how this is special, afaik LDF is analogous to van der Waals force? Is this basically the same as a “loose” active site? (Ie. Can bind a range of similar substrates) Is it because the LDF force acts on an allosteric site of the enzyme and thus changes the active site? I also don’t understand their use of the term “4D”. (Sorry for being difficult, just trying to understand the significance of the paper)

      • Van der Waals is the attraction aspect of LDF, while steric repulsion is the flipside and still a part of LDF interactions. But based on the possible substrates LDF interaction with CYP450, the active site + mechanism of action will adjust to work with what’s around. Not just an allosteric aspect where a select few molecules can fit in the active site. Or at least that’s my understanding of the study’s findings.

        Edit: The 4D aspect is referencing the LDF impact on the enzymes shape and function. LDF impacts all biochem reactions, dipole and hydrophobic forces are a bigger aspect to substrate binding though. But this breaks the mold of what we thought we knew about enzymes and opens the door for a more indepth understanding of biochemical reactions.