The edges of each base pair are exposed in the major and minor grooves, creating a pattern of hydrogen-bond donors and acceptors and of hydrophobic groups (allowing for Vander Waals interactions) that identifies the base pair. The edge of an C : G base pair displays the following chemical groups in the following order in the major groove:

#Question id: 618

#Unit 1. Structure and Function of Biomolecules

 In the following diagram of the first step in the reaction catalyzed by the protease chymotrypsin, the process of general base catalysis is illustrated by the number ________, and the process of covalent catalysis is illustrated by the number _________.

#Question id: 619

#Unit 1. Structure and Function of Biomolecules

The benefit of measuring the initial rate of a reaction V0 is that at the beginning of a reaction:

#Question id: 620

#Unit 1. Structure and Function of Biomolecules

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

#Question id: 621

#Unit 1. Structure and Function of Biomolecules

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:

#Question id: 622

#Unit 1. Structure and Function of Biomolecules

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?

#Question id: 623

#Unit 1. Structure and Function of Biomolecules

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