Chem Test 3

The compound CH₃CH₃NHCH₃ is classified as a

A) primary amine
B) tertiary amine
C) secondary amine
D) hydrated amine
E) quaternary amine

The compound CH₃CH₂NH₂ is classified as a

A) tertiary amine
B) quaternary amine
C) primary amine
D) hydrated amine
E) secondary amine

Which of the following compounds CANNOT form hydrogen bonds with water?

A) (CH₃CH₂)₂NH
B) CH₃CH₂OH
C) (CH₃CH₂)₃N
D) CH₃CH₂NH₂
E) All of the compounds above are capable of forming hydrogen bonds with water

Name the following compound: CH₃-NH-CH₃

a) ethyl amine
b) dimethyl ether
c) methanal
d) 1-methanoate
e) dimethyl amine

In response to allergic reactions or injury to cells, the body increases the production of

A) antihistamine.
B) epinephrine.
C) diphenhydramine.
D) dopamine.
E) histamine.

When acetic acid reacts with ammonia, NH3, the reaction called amidation yields

A) ammonium acetate
B) ethylammonium hydroxide
C) acetamine
D) amino acetate
E) acetamide

In the formation of N-ethylacetamide, the reactant(s) is(are)

A) acetic acid and ethylamine
B) diethylamine
C) acetamide and ethanol
D) ethanol and ethylamine
E) acetic acid and dimethylamine

What relation does the boiling point of an amine have to a simliar hydrocarbon?

A) very similar
B) higher
C) lower

Amines can form _____ bonds with other molecules.

A) metallic
B) oxygen
C) triple
D) hydrogen
E) nonpolar

In what form are amine-containing drugs often administered?

A) amine salt
B) oil solution
C) sodium salt
D) water solution
E) free base

Which of the following is NOT a function of proteins?

A) provide structural components
B) transport substances through the bloodstream
C) catalyze reactions in the cells
D) movement of muscles
E) stores the genetic information of a living organism

Sucrase, the protein that facilitates the hydrolysis of sucrose, would be classified as _____ protein.

A) transport
B) structural
C) hormonal
D) catalytic
E) contractile

The peptide bonds that combine amino acids in a protein are

A) ether bonds
B) ester bonds
C) glycosidic bonds
D) sulfide bonds
E) amide bonds

The bonds that are important in the secondary structure of a protein are

A) hydrophobic interactions
B) peptide bonds
C) disulfide bonds
D) hydrogen bonds
E) salt bridges

Which of the following shows all of the tripeptides that can be formed from one molecule each of glycine (Gly), Valine (Val), and leucine (Leu)?

A) ValGlyLeu & GlyLeuVal
B) GlyValLeu, GlyLeuVal, LeuGlyVal
C) ValGlyLeu, GlyValLeu, GlyLeuVal, LeuGlyVal
D) GlyValLeu, GlyLeuVal, ValLeuGly, ValGlyLeu, LeuGlyVal, LeuValGly
E) GlyValLeu

Hemoglobin has a total of _______ protein chains in its quaternary structure.

A) 4
B) 2
C) 1
D) 5
E) 3

In a typical amino acid zwitterion, the carboxylate end is

A) attached to an amine
B) neutral
C) negatively charged
D) positively charged
E) soluble in a nonpolar solvent

What process occurs when heat, acids, bases, and heavy metal ions cause a los of biological function of a protein?

A) amidation
B) denaturation
C) saponification
D) hydrogenation
E) esterification

In digestion, proteins are broken down into amino acids by a(n) ______ reaction.

A) saponification
B) oxidation
C) denaturation
D) reduction
E) hydrolysis

Which of the following is NOT true for a competitive inhibitor?

A) It can't be converted to products
B) It occupies the active site
C) Increasing the substrate concentration can reverse competitive inhibition
D) It binds to the enzyme at a site remote from the active site.
E) It has a structure similar to the substrate

A noncompetitive inhibitor

A) increases the rate of the enzyme-catalyzed reaction
B) has a structure similiar to the substrate
C) binds at the active site of the enzyme
D) alters the three-dimensional structure of the enzyme

In any reaction catalyzed by an enzyme, the reaction molecule is called the

A) substrate
B) allostere
C) isozyme
D) coenzyme
E) cofactor

When a substance bonds to an enzyme for reaction, its place of binding is the

A) allosteric site
B) primary site
C) primary pocket
D) active site
E) end pocket

In the induced-fit model of enzyme action, the enzyme active site

A) adjusts shape to adapt to the shape of the substrate
B) stays the same shape while causing a change in the shape of the substrate
C) stays the same shape during substrate binding
D) uses an inhibitor to adjust its shape for the substrate
E) uses a cofactor to change the shape of a substrate

The function of the enzyme-substrate complex is to provide an alternative reaction pathway that

A) changes the concentration of the substrate
B) changes the possible product formed
C) lowers the energy of the substrate
D) decreases the activation energy for the reaction
E) lowers the energy of the products

Consider an enzymatic reaction in which the initial concentration of substrate is low. If the amount of enzyme is held constant, but the amount of substrate is increased, the rate of an enzyme catalyzed reaction will

A) increase in an exponential fashion
B) decrease at first, then incrase in a linear fashion
C) stay the same
D) be inhibited by the higher concentrations of substrate
E) increase at first in a linear fashion, then remain at a constant high rate

An irreversible inhibitor is one that

A) forms hydrogen bonds with the substrate
B) reacts covalently with a cofactor
C) binds to the enzyme with hydrophobic interactions
D) binds covalently to the enzyme active site
E) reacts covalently with the substrate

Penicilin functions as an antibiotic by

A) poisoning bacteria with toxins
B) raising the temperature of a bacterium
C) acting as an acetylcholinesterase inhibitor
D) inhibiting the enzymes for cell wall formation in bacteria
E) bonding the metal inons in bacteral electron transport systems

A compound that binds to the surface of an enzyme, and changes its shape so that a substrate cannot enter the active site, is called a(n)

A) competitive inhibitor
B) irreversible inhibitor
C) cofactor
D) noncompetitive inhibitor
E) proenzyme

When an end product from an enzyme-mediated sequence is also an inhibitor for an earlier step in the reaction sequence, the process is referred to as

A) feedback control
B) negative catlysis
C) competitive inhibition
D) concentration control
E) irreversible inhibition

Allosteric enzymes can control their output of product by

A) binding an irreversible inhibitor at the active site
B) changing the pH in the active site
C) reversible inhibition using the product as the inhibitor
D) binding the substrate at a site away from the active site
E) binding a postive or negative regulator at a noncompetitive site

When a cofactor is a small organic molecule, it is known as a(n)

A) zymogen
B) coenzyme
C) regulator
D) isoenzyme
E) vitamin

The B vitamins are examples of

A) vitamnis that are stored in the liver
B) water-soluble vitamins
C) essential amino acids
D) oil soluble vitamins
E) essential minerals

A biological catalyst is called a(n) ______.

A) enzyme
B) cofactor
C) lipid
D) coenzyme
E) substrate

Enzymes that catalyze the same reactions but have slightly different structures are called _____.

A) coenzymes
B) competitive
C) isoenzymes
D) noncompetitive
E) cofactors

A diet very low in vitamin C can lead over time to the condition _______.

A) carpal tunnel syndrom
B) rickets
C) anorexia nervosa
D) cancer
E) scurvy