bioe10-fall05-mt-Conboy_and_Kumar-exam

# bioe10-fall05-mt-Conboy_and_Kumar-exam - BioE 10 Midterm 1....

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BioE 10 Midterm 1. Adenosine triphosphate (ATP) may be hydrolyzed to adenosine diphosphate (ADP) and inorganic phosphate (Pi) with a free energy change ΔG of -7.3 kcal/mol. Suppose you are a molecular bioengineer at a biotech company, and that you have just created a new protein molecular motor which hydrolyzes ATP to perform rotary mechanical work (analogous to F1F0 ATPase). A. You decide to determine the efficiency of the motor by measuring how many revolutions a single molecular motor can make upon hydrolyzing a known number of ATP molecules (similar to Noji et al., 386: 299, 1997). The efficiency of any motor is defined by the ratio of work performed to the energy input. The work of rotation (W) is given by the following product: W=γxΔθ, where γ is the torque of the motor and Δθ is the total angular displacement in radians. If γ = 40 pN*nm and the motor must hydrolyze 25 ATP molecules to make three complete revolutions, what is the efficiency of the motor? (Note 1 rev = 2π radians) B. After characterizing the ATPase activity of your motor, you find that for a given amount of enzyme it has Vmax of 0.834 μmol ADP produced/min and a Km of .334 mM. Assuming Michaelis-Menten kinetics, what initial ATP concentration (in mM) would you need to add to the motor under these conditions to achieve an initial hydrolysis rate of 0.3 μmol/min? C. We discussed in class that cells can produce 30 ATP molecules by aerobically

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## This note was uploaded on 09/16/2009 for the course BIO ENG 10 taught by Professor Lar during the Spring '08 term at Berkeley.

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bioe10-fall05-mt-Conboy_and_Kumar-exam - BioE 10 Midterm 1....

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