TLS Online TPP Program

#Question id: 2127


The fluidity of the lipid side chains in the interior of a bilayer is generally increased by:

#Unit 2. Cellular Organization
  1. a decrease in temperature.

  2. an increase in fatty acyl chain length.

  3. an increase in the number of double bonds in fatty acids.

  4. an increase in the percentage of phosphatidyl ethanolamine

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TLS Online TPP Program

#Question id: 620

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of the following statements about a plot of V0 vs. [S] for an enzyme that follows Michaelis-Menten kinetics is false?

TLS Online TPP Program

#Question id: 621

#Unit 1. Molecules and their Interaction Relevant to Biology

Michaelis and Menten assumed that the overall reaction for an enzyme-catalyzed reaction could be written as Using this reaction, the rate of breakdown of the enzyme-substrate complex can be described by the expression:

TLS Online TPP Program

#Question id: 622

#Unit 1. Molecules and their Interaction Relevant to Biology

An enzyme-catalyzed reaction was carried out with the substrate concentration initially a thousand times greater than the Km for that substrate.  After 9 minutes, 1% of the substrate had been converted to product, and the amount of product formed in the reaction mixture was 12 micromol.  If, in a separate experiment, one-third as much enzyme and twice as much substrate had been combined, how long would it take for the same amount (12 micromol) of product to be formed?

TLS Online TPP Program

#Question id: 623

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of these statements about enzyme-catalyzed reactions is false?

TLS Online TPP Program

#Question id: 624

#Unit 1. Molecules and their Interaction Relevant to Biology

The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: The Km for this enzyme is approximately:

TLS Online TPP Program

#Question id: 625

#Unit 1. Molecules and their Interaction Relevant to Biology

For enzymes in which the slowest (rate-limiting) step is the reaction Km becomes equivalent to: