Allosteric regulation or non-competitive is the same concept. Allosteric means, from the Greek, another place/other space. So, starting by a non-competitive inhibitor, you could design an enzyme like a circle with two separate spots/recesses, symbolising connecting spots, one for the inhibitor and another one for the substrate. When the inhibitor is then placed into its position it changes the conformity of substrate's spot impeding it to connect. For a competitive inhibitor, you could again design an enzyme like a circle but now only with a single binding spot where the inhibitor would connect so the substrate could not. As for the irreversible inhibitor, you could design an enzyme as a circle again but it doesn't matter where you connect the inhibitor, whether on the substrate spot or not, as long as you make clear that there is a strong covalent bond between the enzyme and the inhibitor that doesn't allow the substrate to bind to the enzyme. You could represent this covalent bond by a simple trace connecting the enzyme to the inhibitor: -- .
B press a clean towel or cloth firmly against the cut. you don't want the bleeding to continue and don't want to make the cut worse by putting any liquid in a lab, like acid that could easily be mistaken as water.
Explanation: This is because the same amount of blood that usually goes through will have to fit through a blocked vessel. Only a little will be able to go through at one time, causing the blood flow on the other side to slow.
(That is really dangerous. The build-up will eventually burst the vessel) Just an FYI
Answer: In the middle intertidal, barnacles, mussels and seaweeds all compete for space – a precious limited resource. Mussels are generally the dominant competitor on rocky shores and without the presence of predatory seastars would outcompete other taxa and occupy all available space.
