Biochemistry
Which statement best describes the T state of an allosteric enzyme?
If the allosteric constant L₀ is high, what does this indicate about the equilibrium between T and R states?
How does increasing substrate concentration affect the equilibrium between T and R states in an allosteric enzyme?
How does a decrease in the allosteric constant L₀ affect the sigmoidal nature of an enzyme kinetics curve?
Which model assumes that all subunits of an allosteric enzyme change conformation simultaneously?
According to Le Chatelier's principle, what happens to the equilibrium between T and R states when substrate binds to the R state?
How does positive cooperativity affect the kinetics of allosteric enzymes?
