Tutor profile: Milan A.
What is the difference between gel electrophoresis and SDS-PAGE?
Gel electrophoresis separates DNA, RNA, and proteins by mass and charge without denaturation, whereas SDS-PAGE only separates proteins by mass by applying a uniform negative charge and under denaturing conditions.
An inhibitor binds to the allosteric site of an enzyme while the substrate is attached, locking the substrate into the enzyme-substrate complex. This decreases the Km and Vmax of the reaction. Explain what this means.
This is an example of uncompetitive inhibition. The inhibitor binds to the enzyme-substrate complex, preventing the formation of product. This leads to a decrease in Km because binding affinity has increased, since the substrate is locked tightly to the enzyme. Vmax also decreases because the enzyme is unable to create product, so there are less functional enzymes overall.
Why is Ca+ important for muscle contraction?
Ca+ binds to troponin, causing tropomyosin to expose the binding site
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