Proteins (PPT based) Flashcards
(119 cards)
1
Q
are naturally occurring, unbranched polymer in which the monomer units are amino acids
A
PROTEINS
2
Q
Is a peptide in which at least 40 amino acid residues are present.
A
PROTEINS
3
Q
Examples of PROTEINS:
messengers
A
HORMONES
4
Q
Examples of PROTEINS:
speed up reactions
A
ENZYMES
5
Q
Examples of PROTEINS:
“antinnae”
A
CELL RECEPTORS
6
Q
Examples of PROTEINS:
fight foreign invaders
A
ANTIBODIES
7
Q
Examples of PROTEINS:
allowing specific molecules to enter or leave a cell
A
MEMBRANE CHANNELS
8
Q
the building block of proteins
A
AMINO ACID
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
10
Q
has a structural feature not found in any other standard amino acid.
A
Proline
11
Q
GIV-LAP-MWF
A
NON POLAR AMINO ACID
12
Q
CNS-TQY
A
POLAR NEUTRAL
13
Q
HKR
A
POLAR BASIC
14
Q
DE
A
POLAR ACIDIC
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
16
Q
Synthesized by the body
A
NON-ESSENTIAL AMINO ACIDS
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
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
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
20
Q
symptoms of this disorder includes:
Weight loss, Dehydration, Stomach shrinkage
A
MARASMUS
21
Q
Removes toxic substances released from breakdown of muscle protein during intensive exercise
A
Ala
22
Q
antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants
A
Cys
23
Q
Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules.
A
Gln
24
Q
Component of skin and is beneficial for wound healing. It acts as neurotransmitter
A
Gly
25
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
His
26
It helps promote equilibrium in the central nervous system—aids in balancing state of emotion.
Thr
27
Uncommon amino acids derived from Posttranslational Modification:
found in the cell walls of many bacteria
D-glutamic acid
28
Uncommon amino acids derived from Posttranslational Modification:
found in earthworms
D-serine
29
Uncommon amino acids derived from Posttranslational Modification:
one of the neurotransmitters in the brain
GABA
30
Uncommon amino acids derived from Posttranslational Modification:
a constituent of the vitamin pantothenic acid
β-alanine
31
Glucogenic, Ketogenic, or Both:
glycine, alanine, serine, aspartic acid, asparagine, glutamic acid, glutamine, proline, valine, methionine, cysteine, histidine and arginine
GLUCOGENIC
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Glucogenic, Ketogenic, or Both:
tryptophan, phenylalanine, tyrosine, isoleucine and threonine
BOTH
33
Glucogenic, Ketogenic, or Both:
lysine and leucine
KETOGENIC
34
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
Zwitterion
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NH3+ of the zwitterion loses a proton and negatively charged species is formed
Basic solution
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the zwitterion accepts a proton (H+) to form a positively charged ion
Acidic solution
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the pH at which an amino acid exists primarily in its zwitterion form
ISOELECTRIC POINT
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At the ________, almost all amino acid molecules in a solution (more than 99%) are present in their zwitterion form
isoelectric point
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a covalent bond (amide bond) between the carboxyl group of one amino acid and the amino group of another amino acid.
Peptide bond
40
is an unbranched chain of amino acids, each joined to the next by a peptide bond.
Peptide
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TYPES OF PEPTIDE:
a compound containing two amino acids
dipeptide
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TYPES OF PEPTIDE:
three amino acids joined together in a chain
Tripeptide
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TYPES OF PEPTIDE:
refer to peptides with 10 to 20 amino acid residues.
Oligopeptide
44
TYPES OF PEPTIDE:
long unbranched chain of amino acids, each joined to the next by a peptide bond.
Polypeptide
45
Hormones both produced by the pituitary gland:
1. Oxytocin
2.Vasopressin (ADH)
46
regulates uterine contraction and lactation, plays a role in stimulating the flow of milk in a nursing mother.
Oxytocin
47
regulates the excretion of water by the kidneys
Vasopressin (ADH)
48
Enhances reabsorption of free water also affects blood pressure.
Vasopressin (ADH)
49
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
Enkephalins
50
Antioxidant: regulator of oxidation-reduction reaction
Glutathione
51
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.
Glutathione
52
Bonding in proteins:
the strongest bond
Peptide bond
53
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”
Disulfide bond
54
Bonding in proteins:
result from the attraction of electronegative atoms in the protein molecule. Weaker than the peptide and disulfide bonds.
Hydrogen Bond
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formed between groups which are positively and negatively charge
Ionic bond or salt bridges
56
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
Hydrophobic bond
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is a protein in which only one peptide chain is present.
monomeric protein
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is a protein in which more than one peptide chain is present.
multimeric protein
59
The peptide chains present in multimeric proteins are called _________.
protein subunits
60
is a protein in which only amino acid residues are present.
Simple protein
61
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.
Albumins
62
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.
Globulins
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Based on chemical composition:
Properties:
Soluble in dilute acids and alkalies but insoluble in neutral solvents
Glutelins
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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.
Prolamines
65
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
Histones
66
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
Protamines
67
Based on chemical composition:
Properties:
Insoluble in water and neutral solvents
Scleroproteins (Albuminoids)
68
is a protein that has one or more non-amino acid entities present in its structure in addition to one or more peptide chains
Conjugated protein
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is a non-amino acid group present in a conjugated protein. These non-amino acid components, which may be organic or inorganic
prosthetic group
70
These include substances formed from simple conjugated proteins.
Derived proteins
71
proteins which have undergone slight intramolecular rearrangement through the hydrolytic action of certain physical and chemical agents
Primary Protein derivatives
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synonymous w/ denatured proteins
Primary Protein derivatives
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Product of more extensive hydrolysis
Secondary Protein derivatives
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Mixtures of fragments of original proteins varying in composition and size
Secondary Protein derivatives
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Exhibit certain common properties such as solubility in water and non-coagulability by heat.
Secondary Protein derivatives
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Secondary Protein derivatives:
Soluble in water, precipitated by conc.HNO3 and by half saturation with (NH4)2SO4 or ZnSO4. Not coagulated by heat
Primary proteoses
77
Secondary Protein derivatives:
Precipitated only by complete saturation with (NH4)2SO4 but not with picric acid and HNO3
Secondary proteoses
78
Sequence of amino acids in a protein – that is, the order in which the amino acids are connected to each other
PRIMARY STRUCTURE
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Also involves the order of attachment of the amino acids to each other through covalent peptide bonds
PRIMARY STRUCTURE
80
Is the arrangement in space adopted by the backbone portion of a protein
SECONDARY STRUCTURE
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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.
SECONDARY STRUCTURE
82
Common types of secondary structures:
1. Alpha helix
2. Beta pleated sheet
83
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.
ALPHA HELIX
84
What bond forms between oxygen and hydrogen peptide linkage atoms
Hydrogen bonds
85
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.
TERTIARY
86
Four types of stabilizing interactions contribute to the tertiary structure of a protein:
1. covalent disulfide bonds
2. electrostatic attractions (salt bridges)
3. Hydrogen bonds
4. hydrophobic attractions
87
Is the organization among the various peptide chains in a multimeric protein
QUATERNARY
88
The three-dimensional shape of a protein consisting of two or more independent peptide chains, which results from noncovalent interactions between R groups
QUATERNARY
89
This is also when the protein associates with non-proteic groups. For example, carbohydrates can be added to form a glycoprotein
QUATERNARY
90
Protein whose molecules have an elongated shape with one dimension much longer than the others.
Fibrous
91
Tend to have simple, regular and linear structures.
Fibrous
92
Largely insoluble in ordinary aqueous media, Molecular weights are high, Functions is for structural and support
Fibrous
93
found in wool, feathers, hooves, silk, and fingernails
Keratins
94
found in tendons, bone, and other connective tissue
Collagens
95
found in blood vessels and ligaments
Elastins
96
found in muscle tissue
Myosins
97
found in blood clots
Fibrin
98
Protein whose molecules have peptide chains that are folded into spherical or globular shapes.
Globular
99
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.
Globular
100
Properties:
● Soluble in aqueous media
● Have been crystallized and have definite molecular weights
● Can be denatured
Globular
101
regulatory hormone for controlling glucose metabolism
Insulin
102
involved in oxygen storage in muscles
Myoglobin
103
involved in oxygen, transport in blood
Hemoglobin
104
involved in iron transport in blood
Transferrin
105
involved in immune system responses
Immunoglobulins
106
FIBROUS OR GLOBULAR:
water-insoluble
FIBROUS
107
FIBROUS OR GLOBULAR:
Water-soluble
GLOBULAR
108
FIBROUS OR GLOBULAR:
usually have a single type of secondary structure
FIBROUS
109
FIBROUS OR GLOBULAR:
several types of secondary structure.
GLOBULAR
110
FIBROUS OR GLOBULAR:
generally have structural functions that provide support and external protection
FIBROUS
111
FIBROUS OR GLOBULAR:
involved in metabolic chemistry, performing functions such as catalysis, transport, and regulation.
GLOBULAR
112
FIBROUS OR GLOBULAR:
Lesser in kind of proteins
FIBROUS
113
FIBROUS OR GLOBULAR:
Greater in kind of proteins
GLOBULAR
114
FIBROUS OR GLOBULAR:
Most abundant in the human body
FIBROUS
115
FIBROUS OR GLOBULAR:
Less abundant in the human body
GLOBULAR
116
FIBROUS OR GLOBULAR:
Greater mass composition
FIBROUS
117
FIBROUS OR GLOBULAR:
Lesser mass composition
GLOBULAR
118
is a protein that is found associated with a membrane system of a cell.
MEMBRANEOUS
119
Soluble in aqueous media, Have been crystallized and have definite molecular weights, Can be denatured
MEMBRANEOUS
