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BIO 024: Biochemistry > Proteins (PPT based) > Flashcards

Proteins (PPT based) Flashcards

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1
Q

are naturally occurring, unbranched polymer in which the monomer units are amino acids

A

PROTEINS

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2
Q

Is a peptide in which at least 40 amino acid residues are present.

A

PROTEINS

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3
Q

Examples of PROTEINS:

messengers

A

HORMONES

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4
Q

Examples of PROTEINS:

speed up reactions

A

ENZYMES

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5
Q

Examples of PROTEINS:

“antinnae”

A

CELL RECEPTORS

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6
Q

Examples of PROTEINS:

fight foreign invaders

A

ANTIBODIES

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7
Q

Examples of PROTEINS:

allowing specific molecules to enter or leave a cell

A

MEMBRANE CHANNELS

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8
Q

the building block of proteins

A

AMINO ACID

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9
Q

is an amino acid in which the amino group and the carboxyl group are attached to the carbon atom

A

a-amino acid

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10
Q

has a structural feature not found in any other standard amino acid.

A

Proline

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11
Q

GIV-LAP-MWF

A

NON POLAR AMINO ACID

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12
Q

CNS-TQY

A

POLAR NEUTRAL

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13
Q

HKR

A

POLAR BASIC

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14
Q

DE

A

POLAR ACIDIC

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15
Q

is a standard amino acid needed for protein synthesis that must be obtained from dietary sources because the human body cannot synthesize it in adequate amounts from other substances.

A

ESSENTIAL AMINO ACIDS

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16
Q

Synthesized by the body

A

NON-ESSENTIAL AMINO ACIDS

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17
Q

occurs in people who have a severe protein deficiency. Children who develop this disorder are often older than children who develop marasmus.

A

KWASHIORKOR

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18
Q

symptoms of this disorder includes:

Inability to grow or gain weight, Edema or swelling of the hands and feet, Stomach bulging

A

KWASHIORKOR

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19
Q

occurs more often in young children and babies. It leads to dehydration and weight loss. Starvation is a form of this disorder

A

MARASMUS

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20
Q

symptoms of this disorder includes:

Weight loss, Dehydration, Stomach shrinkage

A

MARASMUS

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21
Q

Removes toxic substances released from breakdown of muscle protein during intensive exercise

A

Ala

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22
Q

antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants

A

Cys

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23
Q

Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules.

A

Gln

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24
Q

Component of skin and is beneficial for wound healing. It acts as neurotransmitter

A

Gly

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25
Q

Important for the synthesis of red and white blood cells. It is a precursor for histamine which is good for sexual arousal. Improve blood flow

A

His

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26
Q

It helps promote equilibrium in the central nervous system—aids in balancing state of emotion.

A

Thr

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27
Q

Uncommon amino acids derived from Posttranslational Modification:

found in the cell walls of many bacteria

A

D-glutamic acid

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28
Q

Uncommon amino acids derived from Posttranslational Modification:

found in earthworms

A

D-serine

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29
Q

Uncommon amino acids derived from Posttranslational Modification:

one of the neurotransmitters in the brain

A

GABA

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30
Q

Uncommon amino acids derived from Posttranslational Modification:

a constituent of the vitamin pantothenic acid

A

β-alanine

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31
Q

Glucogenic, Ketogenic, or Both:

glycine, alanine, serine, aspartic acid, asparagine, glutamic acid, glutamine, proline, valine, methionine, cysteine, histidine and arginine

A

GLUCOGENIC

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32
Q

Glucogenic, Ketogenic, or Both:

tryptophan, phenylalanine, tyrosine, isoleucine and threonine

A

BOTH

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33
Q

Glucogenic, Ketogenic, or Both:

lysine and leucine

A

KETOGENIC

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34
Q

means double ion Is a molecule that has a positive charge on one atom and a negative charge on another atom but which has no net charge

A

Zwitterion

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35
Q

NH3+ of the zwitterion loses a proton and negatively charged species is formed

A

Basic solution

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36
Q

the zwitterion accepts a proton (H+) to form a positively charged ion

A

Acidic solution

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37
Q

the pH at which an amino acid exists primarily in its zwitterion form

A

ISOELECTRIC POINT

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38
Q

At the ________, almost all amino acid molecules in a solution (more than 99%) are present in their zwitterion form

A

isoelectric point

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39
Q

a covalent bond (amide bond) between the carboxyl group of one amino acid and the amino group of another amino acid.

A

Peptide bond

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40
Q

is an unbranched chain of amino acids, each joined to the next by a peptide bond.

A

Peptide

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41
Q

TYPES OF PEPTIDE:

a compound containing two amino acids

A

dipeptide

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42
Q

TYPES OF PEPTIDE:

three amino acids joined together in a chain

A

Tripeptide

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43
Q

TYPES OF PEPTIDE:

refer to peptides with 10 to 20 amino acid residues.

A

Oligopeptide

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44
Q

TYPES OF PEPTIDE:

long unbranched chain of amino acids, each joined to the next by a peptide bond.

A

Polypeptide

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45
Q

Hormones both produced by the pituitary gland:

A
  1. Oxytocin
    2.Vasopressin (ADH)
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46
Q

regulates uterine contraction and lactation, plays a role in stimulating the flow of milk in a nursing mother.

A

Oxytocin

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47
Q

regulates the excretion of water by the kidneys

A

Vasopressin (ADH)

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48
Q

Enhances reabsorption of free water also affects blood pressure.

A

Vasopressin (ADH)

49
Q

Neurotransmitter: pain killers
(pentapeptide): neurotransmitters or neuromodulators at many locations in the brain and spinal cord and are involved with pain perception, movement, mood, behavior, and neuroendocrine regulation; they are also found in nerve plexuses and exocrine glands of the gastrointestinal tract

A

Enkephalins

50
Q

Antioxidant: regulator of oxidation-reduction reaction

A

Glutathione

51
Q

Antioxidants: protecting cellular contents from oxidizing agents such as peroxides and superoxides (highly reactive forms of oxygen often generated within the cell in response to bacterial invasion) with unusual features.

A

Glutathione

52
Q

Bonding in proteins:

the strongest bond

A

Peptide bond

53
Q

Bonding in proteins:

is a covalent bond between two sulfur. Results from the oxidation of the –SH (sulfhydryl) groups of two cysteine molecules to form “cystine”

A

Disulfide bond

54
Q

Bonding in proteins:

result from the attraction of electronegative atoms in the protein molecule. Weaker than the peptide and disulfide bonds.

A

Hydrogen Bond

55
Q

formed between groups which are positively and negatively charge

A

Ionic bond or salt bridges

56
Q

formed by amino acids like leucine, valine, phenylalanine, tryptophan, and proline which adhere each other forming a “micelle” and which do not mix well with water

A

Hydrophobic bond

57
Q

is a protein in which only one peptide chain is present.

A

monomeric protein

58
Q

is a protein in which more than one peptide chain is present.

A

multimeric protein

59
Q

The peptide chains present in multimeric proteins are called _________.

A

protein subunits

60
Q

is a protein in which only amino acid residues are present.

A

Simple protein

61
Q

Based on chemical composition:

Properties:
a. Soluble in water and dilute neutral salt solution
b. Coagulated by heat and precipitated by full saturation with (NH4)2SO4 but not w/ NaCl except with the presence of acid.

A

Albumins

62
Q

Based on chemical composition:

Properties:
a. Soluble in neutral dilute salt solutions but not in water (Neutral salts refers refer to salts of strong acids and bases as NaCl, MgSO4 and (NH4)2SO4.)
b. Coagulated by heat and can be precipitated from their solutions by half saturation with (NH4)2SO4 and complete saturation with NaCl.

A

Globulins

63
Q

Based on chemical composition:

Properties:
Soluble in dilute acids and alkalies but insoluble in neutral solvents

A

Glutelins

64
Q

Based on chemical composition:

Properties:
a. Insoluble in ordinary solvent (water, dilute salt solutions, dilute acid and alkalies) but soluble in 70% alcohol at about neutral point. b. Not coagulable by heat.

A

Prolamines

65
Q

Based on chemical composition:

Properties:
a. Soluble in water, dilute acids and alkalies but not in ammonia.
b. Not readily coagulated by heat
c. Strongly basic and occur in the tissues in the form of salt combinations with acid substances like the heme of the hemoglobin

A

Histones

66
Q

Based on chemical composition:

Properties:
a. Contain smaller number of amino acids
b. Soluble in water and dilute acids and alkalies
c. Not coagulated by heat

A

Protamines

67
Q

Based on chemical composition:

Properties:
Insoluble in water and neutral solvents

A

Scleroproteins (Albuminoids)

68
Q

is a protein that has one or more non-amino acid entities present in its structure in addition to one or more peptide chains

A

Conjugated protein

69
Q

is a non-amino acid group present in a conjugated protein. These non-amino acid components, which may be organic or inorganic

A

prosthetic group

70
Q

These include substances formed from simple conjugated proteins.

A

Derived proteins

71
Q

proteins which have undergone slight intramolecular rearrangement through the hydrolytic action of certain physical and chemical agents

A

Primary Protein derivatives

72
Q

synonymous w/ denatured proteins

A

Primary Protein derivatives

73
Q

Product of more extensive hydrolysis

A

Secondary Protein derivatives

74
Q

Mixtures of fragments of original proteins varying in composition and size

A

Secondary Protein derivatives

75
Q

Exhibit certain common properties such as solubility in water and non-coagulability by heat.

A

Secondary Protein derivatives

76
Q

Secondary Protein derivatives:

Soluble in water, precipitated by conc.HNO3 and by half saturation with (NH4)2SO4 or ZnSO4. Not coagulated by heat

A

Primary proteoses

77
Q

Secondary Protein derivatives:

Precipitated only by complete saturation with (NH4)2SO4 but not with picric acid and HNO3

A

Secondary proteoses

78
Q

Sequence of amino acids in a protein – that is, the order in which the amino acids are connected to each other

A

PRIMARY STRUCTURE

79
Q

Also involves the order of attachment of the amino acids to each other through covalent peptide bonds

A

PRIMARY STRUCTURE

80
Q

Is the arrangement in space adopted by the backbone portion of a protein

A

SECONDARY STRUCTURE

81
Q

Is a result of hydrogen bonding between carbonyl oxygen atom of a peptide linkage and the hydrogen atom of an amino group of another peptide linkage farther along the backbone.

A

SECONDARY STRUCTURE

82
Q

Common types of secondary structures:

A
  1. Alpha helix
  2. Beta pleated sheet
83
Q

is a protein secondary structure in which a single protein chain adopts a shape that resembles a coiled spring (helix), with the coil configuration maintained by hydrogen bonds.

A

ALPHA HELIX

84
Q

What bond forms between oxygen and hydrogen peptide linkage atoms

A

Hydrogen bonds

85
Q

The overall three-dimensional shape of a protein that results from the interactions between amino acids side chains (R groups) that are widely separated from each other within a peptide chain.

A

TERTIARY

86
Q

Four types of stabilizing interactions contribute to the tertiary structure of a protein:

A
  1. covalent disulfide bonds
  2. electrostatic attractions (salt bridges)
  3. Hydrogen bonds
  4. hydrophobic attractions
87
Q

Is the organization among the various peptide chains in a multimeric protein

A

QUATERNARY

88
Q

The three-dimensional shape of a protein consisting of two or more independent peptide chains, which results from noncovalent interactions between R groups

A

QUATERNARY

89
Q

This is also when the protein associates with non-proteic groups. For example, carbohydrates can be added to form a glycoprotein

A

QUATERNARY

90
Q

Protein whose molecules have an elongated shape with one dimension much longer than the others.

A

Fibrous

91
Q

Tend to have simple, regular and linear structures.

A

Fibrous

92
Q

Largely insoluble in ordinary aqueous media, Molecular weights are high, Functions is for structural and support

A

Fibrous

93
Q

found in wool, feathers, hooves, silk, and fingernails

A

Keratins

94
Q

found in tendons, bone, and other connective tissue

A

Collagens

95
Q

found in blood vessels and ligaments

A

Elastins

96
Q

found in muscle tissue

A

Myosins

97
Q

found in blood clots

A

Fibrin

98
Q

Protein whose molecules have peptide chains that are folded into spherical or globular shapes.

A

Globular

99
Q

The folding in such that most of amino acids with hydrophobic side chains (nonpolar R groups) are in the interior of the molecules and most of the hydrophilic side chains (polar) are on the outside of the molecule.

A

Globular

100
Q

Properties:
● Soluble in aqueous media
● Have been crystallized and have definite molecular weights
● Can be denatured

A

Globular

101
Q

regulatory hormone for controlling glucose metabolism

A

Insulin

102
Q

involved in oxygen storage in muscles

A

Myoglobin

103
Q

involved in oxygen, transport in blood

A

Hemoglobin

104
Q

involved in iron transport in blood

A

Transferrin

105
Q

involved in immune system responses

A

Immunoglobulins

106
Q

FIBROUS OR GLOBULAR:

water-insoluble

A

FIBROUS

107
Q

FIBROUS OR GLOBULAR:

Water-soluble

A

GLOBULAR

108
Q

FIBROUS OR GLOBULAR:

usually have a single type of secondary structure

A

FIBROUS

109
Q

FIBROUS OR GLOBULAR:

several types of secondary structure.

A

GLOBULAR

110
Q

FIBROUS OR GLOBULAR:

generally have structural functions that provide support and external protection

A

FIBROUS

111
Q

FIBROUS OR GLOBULAR:

involved in metabolic chemistry, performing functions such as catalysis, transport, and regulation.

A

GLOBULAR

112
Q

FIBROUS OR GLOBULAR:

Lesser in kind of proteins

A

FIBROUS

113
Q

FIBROUS OR GLOBULAR:

Greater in kind of proteins

A

GLOBULAR

114
Q

FIBROUS OR GLOBULAR:

Most abundant in the human body

A

FIBROUS

115
Q

FIBROUS OR GLOBULAR:

Less abundant in the human body

A

GLOBULAR

116
Q

FIBROUS OR GLOBULAR:

Greater mass composition

A

FIBROUS

117
Q

FIBROUS OR GLOBULAR:

Lesser mass composition

A

GLOBULAR

118
Q

is a protein that is found associated with a membrane system of a cell.

A

MEMBRANEOUS

119
Q

Soluble in aqueous media, Have been crystallized and have definite molecular weights, Can be denatured

A

MEMBRANEOUS

BIO 024: Biochemistry (16 decks)

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