Biochem finals exam (test 1)

Question 1

Both myoglobin and hemoglobin primarily bind oxygen through this ion causing their red color:

Answer 1

Iron II

Question 2

The rate of enzyme-catalyzed reaction stated as product molecules formed per second per enzyme active site is called this:

Answer 2

Km/Turnover Number

Question 3

Compounds acting at the active site of an enzyme slowing them down are called:

Answer 3

Competitive Inhibitor

Question 4

In addition to enthalpy changes in the biochemical reactions, this also contributes to the total free energy change.

Answer 4

Entropy (S)

Question 5

We can tell that Hb has multiple subunits as its saturation graph has this shape:

Answer 5

Sigmoid

Question 6

Gibbs showed that change in G must have this range of values in order for reactions to proceed spontaneously.

Answer 6

Negative Range

Question 7

The principle compound in biochemical systems that provides energy through coupling with enzyme is this:

Answer 7

ATP

Question 8

The set of three amino acids working together in the active site of some proteases are called:

Answer 8

Catalytic Triad

Question 9

When enzymes activate other enzymes, this ensures an abundant response, this is termed:

Answer 9

enzyme cascade

Question 10

This is the main type of covalent modification of enzymes that is NOT reversible:

Answer 10

Protease Cleavage

Question 11

Alpha helices and beta-pleated sheets are components of which aspect of protein structures?

Answer 11

Secondary Structure

Question 12

Enzymes increase the rates of biochemical reactions by decreasing this important parameter.

Answer 12

Activation Energy

Question 13

Which of the following are all aromatic amino acids?

Answer 13

PHE, TRY, TRP

Question 14

Amino acids with an alcohol side chain, such as serine, are most likely to be found engaged in the following interaction with nearby amino acid side chains:

Answer 14

Hydrogen Bonding

Question 15

Valine’s side chain is notoriously hydrophobic, as we saw in our analysis of sickle-cell hemoglobin.Where in any protein will it probably be found?

Answer 15

In the interior of the protein avoiding water

Question 16

Which of the following is most likely to disrupt ionic interactions within proteins?

Answer 16

Heavy Metal Ions

Question 17

Most antibiotics are examples of (or do the following:

Answer 17

Competitive Inhibitors

Question 18

One way hemoglobin differs from myoglobin is that Hb has the following:

Answer 18

Quant Structure

Question 19

Bohr showed that a significant external factor in controlling the binding or release of 02 by Hb is

Answer 19

Acidity

Question 20

A significant implication of our study of hemoglobin and other proteins is that the extent of ligand binding to a protein is proportional to:

Answer 20

Ligand Concentration

Question 21

The value of delta G is used to tell the following about a chemical reaction

Answer 21

reaction conditions at equilibrium

Question 22

Kinases, resulting in the hydrolysis of an ATP, are seldom used for energy transfer, but are more likely to be used in which of the following:

Answer 22

Enzyme Regulation

Question 23

In addition to phosphorylation as a mechanism to control protein activity, this is another way proteins are regulated:

Answer 23

Glycosylation, Proteolytic cleavage, Non-covalent binding of effector molecules, Use of isoenzymes

Question 24

This is the most common of the circulating immunoglobulins, particularly during the secondary response

Answer 24

IgG

Question 25

noncompetitive Inhibitor: What does it do? Where does it bind?

Answer 25

decreases the rate of catalysis, Inhibitor can bind free enzyme or the enzyme-substrate complex. They have two different binding sites.

Question 26

Protease Cleavage: what is protease do?

Answer 26

its an enzyme that hydrolyzes the peptide bonds between amino acids. This allows to proteins to be digested.

Question 27

Enzymatic Cascade: What does it do? What is an example?

Answer 27

This is a type of zymogen activation. This achieves a rapid response due to amplification. Example: Blood clotting

Question 28

What is the hydrophobic effect?

Answer 28

Allows nonpolar molecules to interact with each other. this occurs because water can surround the molecules.

Question 29

What are the four levels of protein structures?

Answer 29

primary, secondary, tertiary, quaternary

Question 30

What is the primary structure?

Answer 30

linked by peptide bonds. “amino acid”

Question 31

What is the secondary structure?

Answer 31

Near one another in a linear sequence. “local folding”

Question 32

What is the tertiary structure?

Answer 32

“Overall folding”

Question 33

What is the quaternary structure?

Answer 33

association of subunits

Question 34

What allows for cooperativity?

Answer 34

subunits and BPG