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An allosteric enzyme made up of protein subunits alternates between active and inactive forms?
true
Distinguish between allosteric activation and cooperativity?
cooperativity is an interaction of the subunits of a protein whereby a conformational change in one subunit is transmitted to all others. allosteric regulation is when an activation molecule bonds to an active site where the subunits join.
What is an enzyme called when it changes shape?
An enzyme is called a denatured enzyme once it changes its shape.
What is the difference between an allosteric enzyme and a non-allosteric enzyme?
An allosteric enzyme has multiple binding sites that can be used to modulate its activity through the binding of effectors or ligands, whereas a non-allosteric enzyme typically only has one active site. Allosteric enzymes can exhibit cooperativity, meaning that binding at one site affects binding at another site, while non-allosteric enzymes do not show this behavior.
A logic gate is an electronic circuit which?
Alternates between 0 and 1
When a plants life cycle alternates between a sporophyte and gametophyte?
photosynthesis
What are the differences between a Premier Answerer and an Alternates Specialist?
A Premier Answerer is recognised for their outstanding answers (only Non-Supervisors may receive this badge), whilst an Alternates Specialist is a member of the Vandal Patrol (Supervisors only) that deals with questions with large amounts of alternates, splitting, rewording and recategorizing the alternates.
What type of volcano alternates between construction and destructive phrase?
A convection volcano.
Best selling street motorcycles?
IT ALTERNATES BETWEEN HONDA AND SUZUKI HERE IN THE STATES.
What is The process in which the CPU alternates communication between two or more memory banks?
interleaving
The lifecycle of plants alternates between?
a haploid gametophyte stage and a diploid sporophyte stage..
What is the difference between a noncompetitive inhibitor and an allosteric inhibitor in enzyme regulation?
A noncompetitive inhibitor binds to an enzyme at a site other than the active site, while an allosteric inhibitor binds to a different site on the enzyme, causing a change in the enzyme's shape and reducing its activity.
