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22-23 Flashcards

1
Q

are giant molecules made of amino acids
linked together by peptide bonds

A

Proteins

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2
Q

Proteins are giant molecules made of amino acids
linked together by

A

peptide bonds

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3
Q

Proteins have many functions

A

structural (collagen), enzymatic, carrier (hemoglobin), storage (casein), protective (immunoglobulin), and hormonal (insulin)

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4
Q

are organic compounds containing an
amino and a carboxylic acid group

A

Amino acids

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5
Q

All amino acids in human tissues are

A

L-amino acids.

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6
Q

Amino acids in the solid state, as well as in water,
carry both positive and negative charges

A

zwitterions

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7
Q

The pH at which the number of positive charges
equals the number of negative charges is the

A

electric point of an amino acid or protein

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8
Q

Amino acids are nearly identical in most ways except
for their

A

side chain (R ) groups

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9
Q

gives an
amino acid its particular properties

A

unique nature of the side chain

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9
Q

they are precursors of
neurotransmitters

A

aromatic amino acids (Phe, Tyr, Trp)

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10
Q

Some amino acids have charged side chains

A

(Glu, Asp, Lys, Arg, His).

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11
Q

amino group of one amino acid condenses
with the carboxyl group of another amino acid

A

amide (peptide) bond is formed

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11
Q

short-range conformation

A

(a-helix, b-pleated sheet, extended helix of collagen,
and random coil

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11
Q

___ a special amino acid because its side
chain ( SH) can form disulfide bridges with another
____

A

Cysteine

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12
Q

is the three-dimensional
conformation of the protein molecule

A

tertiary structure

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12
Q

linear sequence of amino acids is the

A

primary structure

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12
Q

repeating short-range conformations

A

secondary structures

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12
Q

largely responsible for the
eventual higher-order structures of proteins

A

primary structure

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12
Q

Two amino acids form a

A

dipeptide

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13
Q

Tertiary structures are maintained by covalent cross links such as

A

disulfide bonds and by salt bridges,
hydrogen bonds, metal ion coordination, and
hydrophobic interactions between the side chains.

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13
Q

refers to those repetitive structures that are held together via hydrogen bonds
between groups on the peptide backbone only

A

Secondary structure

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13
Q

precise fit of polypeptide subunits into an aggregated whole is called the

A

quaternary structure

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13
Q

proteins with quaternary structure

A

proteins that have subunits

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14
Q

stabilize the native
conformations of proteins.

A

Secondary and tertiary structures

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14
Q

destroy these structures and denature proteins

A

Physical and chemical agents, such as heat or urea

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15
Q

A large biological molecule made of numerous amino acids linked by amide bonds

A

Protein

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15
Q

“of first importance,”

A

proteios

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15
Q

“protein” is derived from the Greek

A

proteios

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16
Q

by far the most important of all biological compound

A

Proteins

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16
Q

roles of protein

A
  1. Structure
  2. Catalysis
  3. Movement
  4. Transport
  5. Hormones
  6. Protection
  7. Storage
  8. Regulation
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17
Q

Two important structural proteins

A

collagen and keratin

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18
Q

Muscles are made up of protein molecules

A

myosin and actin

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19
Q

a protein in the blood, carries oxygen from the
lungs to the cells in which it is used and carbon dioxide from the cells to
the lungs

A

hemoglobin

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19
Q

protein from an outside source or some other foreign substance

A

antigen

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20
Q

proteins to counteract the foreign protein

A

antibodies

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20
Q

a protein in the liver, stores

A

Ferritin, iron

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21
Q

proteins into two major types

A

fibrous proteins, globular proteins

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22
Q

type of protein that are insoluble in water and are used mainly for structural purposes

A

fibrous proteins

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23
Q

type of protein that are more or less soluble in water and are used mainly for nonstructural purposes

A

globular proteins

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24
Q

An amino acid in which the amino group is
linked to the carbon atom next to the COOH carbon

A

Alpha (a) amino acid

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25
Q

attracted to water

A

hydrophilic

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25
Q

they repel water

A

hydrophobic

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25
Q

reaction can take place between a primary amine and an aldehyde or a ketone, not catalyzed by enzymes

A

glycation

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25
Q

A very important tripeptide present in high concentrations in all tissues is

A

Glutathione

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26
Q

Compounds that have a positive charge on one atom and a negative charge on another are called

A

zwitterions

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26
Q

“hybrid.”

A

zwitter

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27
Q

contains L-glutamic acid, L-cysteine,
and glycine

A

Glutathione

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27
Q

A pH at which a sample of amino acids or protein has an equal number of positive and negative charges

A

Isoelectric point (pI)

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27
Q

The amino acid at the
end of a peptide that has a free
a-carboxyl group

A

C-terminus

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28
Q

functions in the cells as a general protective agent

A

Glutathione

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29
Q

The amino acid at the
end of a peptide that has a free
a-amino group

A

N-terminus

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29
Q

ways to combat the harmful effects
of AGEs

A

use antioxidants,

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30
Q

high-molecular-weight, water-insoluble,
brownish complexes

A

advanced glycation end-products (AGE).

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30
Q

The longer we live, and the higher the blood sugar concentration becomes, the ___ AGE products accumulate in the body

A

more

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30
Q

insulin reaction

A

hypoglycemia

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30
Q

a very serious disease that happens when there;s different kind of hemoglobin in blood

A

, sickle cell anemia.

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31
Q

hypoglycemic awareness

A

hunger, sweating, and poor coordination

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31
Q

repeating pattern classified as a secondary structure is the

A

extended helix of collagen

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32
Q

prompts the bone marrow to manufacture fetal hemoglobin

A

Hydroxyurea

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32
Q

Salt bridges

A

electrostatic attraction

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33
Q

most often involved in stabilization of the tertiary structure of proteins is the disulfide bond

A

Covalent Bonds

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34
Q

secondary structures are stabilized by hydrogen bonding between backbone C O and N H groups.

A

Hydrogen Bonding

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34
Q

prions undergo conformational change,
they can cause diseases such as

A

mad cow disease and scrapie in
sheep

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34
Q

A protein that helps other proteins to fold into the
biologically active conformation and enables partially denatured proteins to regain their biologically active conformation

A

Chaperone

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35
Q

are small proteins found in nerve tissue, although their exact function remains a mystery

A

prions

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36
Q

prion

A

Stanley Prusiner

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36
Q

holds much promise for the future of
protein analysis

A

protein microarray

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37
Q

Proteins that contain
non-amino acid portions are called

A

conjugated proteins

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37
Q

used for mass determination and can be
adapted for protein identification

A

Mass spectrometry

37
Q

complement of proteins
expressed by a genome is called

A

proteome

37
Q

acid portion of a conjugated protein is called

A

prosthetic group

38
Q

The loss of the secondary, tertiary, and quaternary structures of a protein by a chemical or physical agent that leaves the primary structure intact

A

Denaturation

38
Q

these noncovalent interactions, subtle changes in structure at one site on a protein molecule may cause drastic changes in properties at

A

allosteric proteins

38
Q

are macromolecules that catalyze chemical
reactions in the body

A

Enzymes

39
Q

they catalyze only one particular reaction

A

Enzymes

39
Q

compound whose reaction is catalyzed by an
enzyme is called the

A

substrate

39
Q

Most enzymes are

A

proteins, although some are made of RNA.

40
Q

Some enzymes are made of

A

polypeptide chains only

40
Q

besides the polypeptide chain

A

apoenzyme

41
Q

nonprotein

A

cofactors

41
Q

organic compounds

A

coenzymes

41
Q

part of the enzyme surface that participates in the actual catalysis of chemical reactions

A

active site

42
Q

are part of the active site

A

Cofactors

42
Q

Compounds that slow enzyme action are called

A

inhibitors

42
Q

attaches itself to the active site

A

competitive inhibitor

43
Q

the concentration of products influences the rate of the reaction

A

feedback control

43
Q

binds to other parts of the enzyme surface

A

noncompetitive inhibitor

43
Q

the enzyme and substrate concentrations and enzyme activity relationship

A

directly proportional

43
Q

an interaction takes place at a position other than the active site but affects the active site, either positively or negatively

A

allosterism

43
Q

Enzyme activity is regulated by

A

five mechanisms

44
Q

has its greatest activity

A

optimal temperature and pH

44
Q

Enzymes ___ the activation energy required for
a biochemical reaction to occur.

A

lower

44
Q

must be activated by removing a small portion of the
polypeptide chain

A

proenzymes or zymogens

44
Q

Two closely related mechanisms that seek to explain
enzyme activity and specificity are

A

lock-and-key model and the induced-fit model.

45
Q

Enzymes can be activated or inhibited by

A

protein modification

46
Q

can be used to diagnose certain diseases

A

Abnormal enzyme activity

47
Q

Enzyme activity is also regulated by _____ which are different forms of the same enzyme

A

isozymes

48
Q

active site of an enzyme favors the production of
the

A

transition state

49
Q

Molecules that mimic the transition state are called

A

transition-state analogs

50
Q

they make potent enzyme inhibitors.

A

transition-state analog

51
Q

are enzymes made of ribonucleic acids

A

Ribozymes

52
Q

The limitation of an enzyme to catalyze specific reactions with specific substrates

A

Substrate specificity

52
Q

an enzyme that cleaves the peptide bonds of protein molecules—but not every peptide bond

A

trypsin

53
Q

neurotransmitter that operates between the nerve
endings and muscles

A

Acetylcholine

53
Q

muscle relaxants

A

Acetylcholine, Succinylcholine

54
Q

catalyze oxidations and reductions.

A

Oxidoreductases

55
Q

catalyze the transfer of a group of atom

A

Transferases

55
Q

catalyze hydrolysis reactions

A

Hydrolases

55
Q

catalyze isomerization reactions

A

Isomerases

55
Q

catalyze the joining of two molecules

A

Ligases, or synthetases

55
Q

catalyze the addition of two groups to a double bond or the removal of two groups from adjacent atoms to create a double bond

A

Lyases

55
Q

Aspartate amino transferase

A

Transferases

55
Q

Lactate dehydrogenase

A

. Oxidoreductases

56
Q

Acetylcholinesterase

A

Hydrolases

56
Q

A nonprotein organic
molecule, frequently a B vitamin,
that acts as a cofactor

A

Coenzyme

56
Q

aspartate transaminase

A

Transferases

56
Q

Tyrosine-tRNA synthetase

A

Ligases

56
Q

Aconitase

A

Lyases

57
Q

Phosphohexose isomerase

A

isomerase

57
Q

The nonprotein part
of an enzyme necessary for its
catalytic function

A

Cofactor

58
Q

A three-dimensional
cavity of the enzyme with specific
chemical properties that enable
it to accommodate the substrate

A

Active site

59
Q

A compound that binds
to an enzyme and lowers its
activity

A

Inhibitor

60
Q

measure of how much reaction rates are increased

A

Enzyme activity

61
Q

suggested that catalysts speed up reactions by combining with the substrate to form some kind of intermediate compound, this intermediate is called the

A

enzyme–substrate complex.

61
Q

A model explaining the specificity of enzyme action by comparing the active site to a lock and the substrate to a key

A

Lock-and-key model

62
Q

A model explaining the specificity of enzyme action by comparing the active site to a glove and the substrate to a hand

A

Induced-fit model

63
Q

assumes that the enzyme is a rigid, three-dimensional body

A

lock-and-key model

63
Q

surface that contains the active site has a restricted opening into which only one kind of substrate can fit

A

lock-and-key model

64
Q

was the first to explain the action of enzymes

A

lock-and-key model

65
Q

the enzyme modifies the shape of the active site to accommodate the substrate

A

induced-fit model

65
Q

Daniel Koshland

A

induced-fit model

66
Q

organisms can live in an extreme pH environment

A

Helicobacter pylori

67
Q

a live under the mucus coating of the stomach and release a toxin that causes ulcers and has been linked to stomach cancer

A

Helicobacter pylori

68
Q

a protective, neutralizing basic cloud in the H. pylori

A

urease

68
Q

urease in H. pylori

A

found on the surface of the bacteria, is protected against acid denaturation by its quaternary structure

69
Q

energy required to climb this hill is the

A

activation energy

70
Q

key strategy in the treatment of acquired immunodeficiency syndrome (AIDS

A

develop specific inhibitors that selectively block the actions of enzymes unique to the human immunodeficiency virus

70
Q

A chemical reaction where an electron-rich atom, such as oxygen or sulfur, bonds to an electron-deficient atom, such as carbonyl carbon

A

nucleophilic attack

71
Q

an enzyme essential to the production of new virus particles in infected cells (AIDS)

A

HIV protease

71
Q

site to which regulator attaches is called

A

regulatory site

71
Q

more active form is

A

R form, where “R” stands for relaxed

71
Q

an enzyme regulation process in which formation of a product inhibits an earlier reaction in the sequence

A

Feedback control

71
Q

inhibit enzyme action

A

negative modulation

71
Q

A protein that becomes an active enzyme
after undergoing a chemical change

A

Proenzyme (zymogen)

72
Q

usually a change in the primary structure, typically
by addition of a functional group covalently bound to the apoenzyme

A

protein modification.

72
Q

An enzyme in
which the binding of a regulator
on one site on the enzyme modifies
the enzyme’s ability to bind the
substrate in the active sit

A

Allosteric enzyme

73
Q

may stimulate enzyme action

A

positive modulation

73
Q

substance that binds to the allosteric enzyme is called

A

regulator

74
Q

Alanine amino- transferase (ALT)

A

Hepatitis

74
Q

less active form

A

T form, where “T” stands for taut

74
Q

Acid phosphatase

A

Prostate cancer

75
Q

Enzymes
that perform the same function
but have different combinations
of subunits and thus different
quaternary structures

A

Isozymes (Isoenzymes)

75
Q

Alkaline phosphatase (ALP)

A

Liver or bone disease

75
Q

Amylase

A

Pancreatic disease or mumps

75
Q

Creatine phosphokinase (CPK)

A

Heart attack

75
Q

Aspartate amino transferase (AST)

A

Heart attack or hepatitis

76
Q

Phosphohexose isomerase (PHI)

A

Heart attack

76
Q

Lactate dehydrogenase (LDH)

A

Heart attack

77
Q

, an enzyme that breaks down glycogen

A

glycogen phosphorylase

77
Q

a dimer controlled by modification and by allosterism.

A

Glycogen phosphorylase

77
Q

common way to attempt to treat the addiction is to

A

use a compound that blocks the receptor and denies the drug access to it

77
Q

Two forms of phosphorylase exist called

A

phosphorylase b and phosphorylase a

77
Q

created the first catalytic antibodies

A

Richard Lerner and Peter Schult

77
Q

operate by binding to a particular receptor in the neurons, mimicking the action of a neurotransmitter

A

addictive drugs

77
Q

catalyzes the conversion of arachidonic acid to PGH

A

prostaglandin enderoperoxide synthase

78
Q

An antibody that has
catalytic ability because it was
created by using a transition-state analog as an immunogen

A

Abzyme

78
Q

prostaglandin enderoperoxide synthase has two distinct functions

A

The enzyme’s cyclooxgenase activity is to close a substituted cyclopentane ring. The peroxidase activity of the same enzyme yields the 15-hydroxy derivative prostaglandin, PGH2

78
Q

Degradation of cocaine by esterases or catalytic antibodies

A

Cocaine (a) passes through a transition state

(b) on its way to being hydrolyzed to benzoic acid and ecgonine methyl ester

(c). Transition-state analogs are used to generate catalytic antibodies for this reaction.

78
Q

an enzyme that hydrolyzes an ester bond that is part of cocaine’s structure

A

specific esterase

79
Q

blocks the reuptake of the neurotransmitter dopamine

A

cocaine

80
Q

antibodies successfully hydrolyze cocaine to
two harmless degradation products

A

benzoic acid and ecgonine

80
Q

mechanism of action of cocaine

A

(a) Dopamine acts as a neurotransmitter. It is released from the presynaptic neuron, travels across the synapse, and bonds to dopamine receptors on the postsynaptic neuron. It is later released and taken up into vesicles in the presynaptic neuron.
(b) Cocaine increases the amount of time that dopamine is available to
the dopamine receptors by blocking its uptake

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