Yet properties of the molecule — in particular involving
the charge of its active site — have stymied potential developers of inhibitors.
Not exact matches
Most importantly, they found that the
active site of TTLL7 is ideally positioned to contact the negatively
charged «beta - tail»
of beta - tubulin, one
of the two protein building blocks
of the microtubule polymer (alpha - and beta - tubulin).
The researchers knew they needed a catalyst that could not only support
active and efficient chemical reactions, but one that could also provide a stable interface with the semiconductor, allow the
charge generated by the absorption
of light from the semiconductor to be efficiently transferred to the
sites doing catalysis, and permit as much light as possible to pass through.
This has been viewed as a «relaxation»
of the enzyme
active site that is
charged with iron - hydrides that are needed for the N2 reduction reaction.