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Biochemistry > Proteins > Flashcards

Proteins Flashcards

1
Q

Protein, Nitrogen, Sulfur

A

Major Classes of Food Molecules

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1
Q

Meaning “Of first importance”

A

Protein

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2
Q

available from fats and carbohydrates

A

Carbon and Hydrogen

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3
Q

Unavailable from fats and carbohydrates

A

Nitrogen and Sulfur

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4
Q

biological catalysts and mostly are in proteins

A

Enzymes

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5
Q
  • antibodies or immunoglobulins
A

Defense proteins

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6
Q

bacteria and viruses that infect the body

A

antigens

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7
Q

carry materials from one place to another

A

transport proteins

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8
Q

transports iron. from the liver to the bone marrow

A

Transferrin

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9
Q

transport of oxygen in higher organisms

A

hemoglobin

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10
Q

storage of oxygen in higher organisms

A

myoglobin

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11
Q

control many aspects of cell function

A

regulatory proteins

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12
Q
  • mechanical support to large animals
  • mechanical strength for our bones, tendons, and skin
A

structural proteins

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13
Q

found in hair and fingernails

A

Keratin

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14
Q

necessary for all forms of movement

A

movement proteins

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15
Q

contract and expand the heart

A

actin and myosin

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16
Q

most important muscle

A

heart

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17
Q

sources of amino acids for embryos or infants

A

nutrient proteins

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18
Q
  • found in milk
  • nutrient storage of proteins
A

Albumin and Casein

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19
Q

protein that are made up of some combination of twenty different sub-units

A

a- amino acids

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20
Q
  • (-COO)
  • carboxyl group that has lost a proton
A

Carboxylate group

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21
Q

conjugate base form

A

Carboxylate group

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22
Q

amino group that has gained a proton

A

Protonated amino group

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23
Q

conjugate acid form

A

Protonated amino group

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24
Q

it interacts with one another through a variety of weak attractive forces

A

R group

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25
Q

19 of the 20 amino acids

A

Primary amines on the a-carbon

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26
Q

what kind of amine is Proline

A

Secondary amine

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27
Q

pH required for life functions

A

pH 7

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28
Q

neutral molecule with equal numbers of positive and negative charges

A

Zwitterions

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29
Q

pH where there is no net charge on zwitterions

A

Isoelectric point

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30
Q

amino acids in water exist as dipolar ions

A

Zwitterions

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31
Q

have mirror-image forms or enantiomers

A

chiral

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32
Q

two hydrogen atoms attached to the a-carbon

A

glycine

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33
Q

determine which is D- and which is L-

A

N+H3 group

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34
Q
  • carboxyl group
  • found at the top of the molecule
A

Most oxidized end in D-L notation

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35
Q

absolute configuration of amino acids in protein

A

L stereoisomers

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36
Q

Almost all monosaccharides found in nature

A

D- family

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37
Q

almost all of the a-amino acids isolated from proteins in nature

A

L - family

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38
Q
  • non polar
  • prefer contact with one another over contact with water
  • stabilize the protein by hydrophobic interactions
A

Hydrophobic Amino acids

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39
Q

What are the 9 hydrophobic amino acids

A
  • alanine
  • valine
  • leucine
  • isoleucine
  • proline
  • glycine
  • methionine
  • phenylalanine
  • tryptophan
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40
Q

what amino acid that the R group is unique

A

Proline

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41
Q
  • polar
  • attracted to polar water molecules
  • on the surfaces of proteins
A

hydrophilic amino acids

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42
Q
  • not ionic at pH 7
  • most associate with one another by hydrogen bonding
A

polar, neutral amino acids

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43
Q

form disulfide bonds with one another

A

cysteine molecules

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44
Q

6 amino acids that are polar and neutral

A
  • serine
  • threonine
  • tyrosine
  • cysteine
  • asparagine
  • glutamine
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45
Q
  • ionized carboxyl groups in their side chains
  • net charge of -1 at pH 7
A

negatively charged amino acids

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46
Q

2 amino acids that are negatively charged

A

aspartate and glumate

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47
Q
  • net positive charge at pH 7
  • side chains contain positive groups
A

Positively charged amino acids

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48
Q

side chains react with water, picking up a proton and releasing a hydroxide anion

A

basic amino acids

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49
Q

ionization of the carboxylic acid releases a proton

A

acidic amino acids

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50
Q

what are the 3 positively charged amino acids

A

lysine , arginine , histidine

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51
Q

where is asparagine first found

A

asparagus

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52
Q

where is tyrosine first found

A

cheese

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53
Q

what the glykos means in glycine

A

sweet

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54
Q

it is the amide bond between - COO group and a-N+H3

A

peptide bond

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55
Q

it is where water molecule is lost and the amide bond is formed

A

condensation reaction

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56
Q
  • linear polymers of L-a-amino acids
  • it is the carboxyl group of one amino acid that is linked to the amino group of another amino acid
A

Proteins

57
Q

molecule formed by condensing two amino acids

A

dipeptide

58
Q
  • amino acid with a free α-N⁺H3 group
  • amino terminal
  • written on the left
A

N - terminus

59
Q
  • amino acid with a free —COO− group
  • carboxyl terminal
  • written on the right
A

C - terminus

60
Q

carbon-1

A

carboxyl group

61
Q

carbon-2

A
  • α-carbon
  • always bonded to a hydrogen atom
  • always bonded to the R group side chain
62
Q

N

A

a-amino group

63
Q
  • both planar (flat) and rigid
  • partially double bond character
  • exhibits resonance
A

Peptide bonds

64
Q

dictated by the sequence of the gene

A

sequence of amino acid residues

65
Q
  • depend on the location of those R groups along the chain
  • govern how the protein chain folds
  • dictates its final three-dimensional structure and its biological function
A

interactions among the R groups

66
Q
  • regions of the primary sequence of a protein fold into regularly repeating structures
  • stable arrangements of amino acid residues giving rise to polypeptide folds of repeating structure
A

secondary structure of proteins

67
Q

maximize hydrogen bonding in the backbone

A

α-helix or β-pleated sheet

68
Q

two regions of a protein chain that may have different types of secondary structure

A

random or nonregular structure and α-helix or β-pleated sheet

69
Q
  • most common
  • coiled, helical conformation
A

a-Helix

70
Q

Every amide hydrogen and carbonyl oxygen associated with the peptide backbone

A

involved in a hydrogen bond

71
Q

hydrogen-bonded to an amide hydrogen 4 amino acids away in the chain

A

every carbonyl oxygen

72
Q

parallel to the long axis of the helix

A

hydrogen bonds

73
Q

Repeat distance of the helix, or its pitch

A

5.4 angstroms (A)

74
Q

amino acids per turn of the helix

A

3.6

75
Q
  • structural proteins arranged in fibers or sheets that have only one type of secondary structure
  • give strength and flexibility to the structure
  • insoluble in water
A

fibrous proteins

76
Q
  • high concentration of hydrophobic amino acids
  • mechanical strength, structural components, movement
A

fibrous proteins

77
Q
  • form the covering of most land animals
  • hair, wool, nails, hooves, and fur
  • protofilaments and protofibrils
  • right handed and coiled
A

a - keratins

78
Q
  • found in connective tissues such as tendons, cartilage, bone, cornea
  • left handed and coiled
A

collagen

79
Q

proteins consist almost exclusively of polypeptide chains coiled up into α-helices

A

hair

80
Q
  • three-stranded superstructure formed from a single α helix coiled in a bundle with two other helices
  • part of an array known as microfibril
  • resemble “molecular pigtails”
A

protofibril

81
Q
  • great mechanical strength
  • virtually insoluble in water
A

protofibril

82
Q
  • pleated folds of drapery
  • carbonyl oxygens and amide hydrogens are involved in hydrogen bonds
A

B - pleated sheet

83
Q
  • structure is stabilized by extensive H-bonding and van der Waals interaction between sheets
  • polypeptide chain is nearly completely extended
A

B - pleated sheet

84
Q
  • N-termini are head to head
A

parallel B-pleated sheet

85
Q
  • N-terminus of one chain is aligned with the C-terminus of a second chain
  • head to tail
A

antiparallel B-pleated sheet

86
Q
  • produced by silk-worms, insects, and spiders
  • protein whose structure is an antiparallel β-pleated sheet
A

Silk fibroin

87
Q
  • does not stretch because the beta conformation is already highly extended
  • flexible because the sheets are held by weak interaction rather than by covalent bonding such as disulfide bonds
A

silk

88
Q

accounts for nearly half of the amino acids of silk fibroin

A

glycine

89
Q
  • account for most of the others
  • Methyl groups of alanines and hydroxymethyl groups of serines
A

alanine and serine

90
Q
  • most fibrous proteins
  • majority of cellular proteins
  • globular proteins
A

tertiary structure of proteins

91
Q
  • soluble proteins
  • have the tertiary structure
  • extremely compact
A

globular proteins

92
Q
  • include enzymes, transport proteins, regulatory proteins, immunoglobulins, and other proteins with diverse functions
  • 3-dimensional structures are still being known
A

globular proteins

93
Q
  • three-dimensional shape of the entire peptide chain
  • regions of secondary structure, α-helix and β-pleated sheet, further fold on themselves to achieve the tertiary structure
A

tertiary structure

94
Q
  • defines the biological function of proteins
  • forms spontaneously
  • maintained as a result of interactions among the R groups
A

tertiary structure

95
Q

What molecular interactions
- London dispersion forces
- dipole-dipole attractions
- between hydrophobic or nonpolar R groups

A

van der waals forces

96
Q

What molecular interactions has between polar R groups

A

hydrogen bonds

97
Q

what molecular interactions has
- between oppositely charged R groups
- between ionic side chains -COO and -NH3

A

ionic bonds (salt bridges)

98
Q

what molecular interactions has between the thiol-containing amino acid residues

A

covalent bonds

99
Q
  • association of several polypeptides to produce a functional protein
  • arrangement of multiple polypeptide subunits to form the larger protein that can serve a variety of functions
A

quarternary structure

100
Q

what holds the quarternary structure of a protein that also holds the tertiary structure

A

molecular interactions

101
Q
  • non-amino acid part of a conjugated protein
  • some quaternary structure involves binding to a nonprotein group
  • often determines the function of a protein
A

prosthetic group

102
Q
  • proteins with sugar groups covalently attached
  • many of the receptor proteins on cell surfaces
A

glycoproteins

103
Q
  • each of the subunits of hemoglobin is bound to an iron-containing heme group
  • large, unsaturated organic cyclic amine with an iron ion coordinated within it
  • ability to bind reversibly to oxygen
A

Heme group

104
Q
  • found in red blood cells
  • oxygen transport protein of higher animals
  • each contains a heme group which can hold 1 molecule of oxygen
A

hemoglobin

105
Q
  • only slightly soluble in aqueous solutions
  • transferred from hemoglobin to myoglobin as myogolobin has a stronger attraction for oxygen than hemoglobin
A

oxygen

106
Q

tetramer composed of four polypeptide subunits

A
  • 2 α-subunits
  • 2 β-subunits
107
Q
  • greater affinity for oxygen than does the mother’s hemoglobin
  • oxygen is therefore efficiently transported via the circulatory system
A

fetal hemoglobin

108
Q
  • sickled appearance of the red blood cells
  • unable to pass through the small capillaries of the circulatory system
A

sickle cell hemoglobin

109
Q
  • in the β-chain of sickle cell hemoglobin
  • hydrophobic amino acid
  • replaced a glutamic acid
A

valine

110
Q
  • one normal gene and one defective gene
  • produce both normal and altered β-chains
  • 50% chance of passing the gene
A

sickle cell trait

111
Q
  • 90% water and 10% solutes
  • 70% of the plasma solid are plasma proteins
  • contains 60–80 grams per liter (g/L) of proteins
A

blood plasma

112
Q
  • most abundant protein in the blood
  • contributes to the osmotic pressure of the blood
    • because it is a dissolved molecule
A

albumin

113
Q

waste product of the breakdown of hemoglobin

A

Bilirubin

114
Q

transport protein for free hemoglobin

A

haptoglobin

115
Q

copper transport protein

A

ceruloplasmin

116
Q

blood clotting

A

prothrombin

117
Q

proteins with sugar groups

A

glycoproteins

118
Q
  • most abundant α₁-globulin
  • inactivation of an enzyme that causes damage in the lungs
A

α₁-Antitrypsin

119
Q
  • inhibitor found in the bloodstream
  • found in the amyloid plaques characteristic of Alzheimer’s disease (AD), along with amyloid proteins
A

α₁-Antichymotrypsin

120
Q
  • 7% of the plasma protein
  • coagulation of blood
A

fibrinogen

121
Q

where most of the remaining plasma proteins are synthesized

A

liver

122
Q
  • organized structures of a globular protein become completely disorganized
    • α-helix, the β-pleated sheet, and tertiary folds
  • does not alter the primary structure
A

denaturation

123
Q
  • breaking down into smaller peptides or amino acids
  • changes in pH
  • enzymes
  • temperature
A

hydrolysis

124
Q
  • breaking up the 3D shape
  • temperature
    • as the temperature increases further, the bonds within the protein vibrate more violently
  • heavy metals
  • detergents
  • organic solvents
  • ## mechanical stress
A

denaturation

125
Q
  • protein molecules then unfold and become entangled
  • no longer in solution
  • aggregated to become a solid
  • will precipitate out of the solution
A

coagulation

126
Q

have both a hydrophobic region (fatty acid tail) and a polar or hydrophilic region

A

detergent

127
Q
  • stomach enzyme
  • begins the digestion by hydrolyzing some of the peptide bonds
  • breaks the protein down into smaller peptides
  • Production of pepsin and other proteolytic digestive enzymes
A

pepsin

128
Q

cleaves peptide bonds on the carbonyl side of aromatic amino acids

A

chymotrypsin

129
Q

carbonyl side of basic amino acids

A

trypsin

130
Q
  • cannot be synthesized by the body
  • required in the diet
A

essential amino acids

131
Q

what are the essential amino acids

A

isoleucine, leucine, lysine, methionine, threonine, tryptophan, valine

132
Q
  • can be synthesized by the body
  • need not be included in the diet
A

non-essential amino acids

133
Q

what are the non-essential amino acids

A

alanine, arginine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, histidine, proline, serine, tyrosine

134
Q
  • protein derived from animal sources
  • provides all of the essential and nonessential amino acids in approximately the correct amounts for biosynthesis
A

complete protein

135
Q
  • protein derived from vegetable or plant sources
  • lacks a sufficient amount of one or more essential amino acids
A

incomplete protein

136
Q
  • major protein contains lysine and tryptophan
  • very little methionine
A

beans

137
Q
  • contains considerable methionine
  • very little tryptophan or lysine
A

corn

138
Q
  • inactive form of pepsin
  • additional forty-two amino acids in its primary structure
  • removed in the stomach to produce active pepsin
A

pepsinogen

139
Q

dimeric amino acid as a result of the oxidation of 2 polar cysteines

A

cystine

Biochemistry (5 decks)

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