Proteins Flashcards

(104 cards)

1
Q

-simple organic compounds that serve as the building blocks of proteins

A

AMINO ACIDS

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2
Q

-Amino acids are amphoteric and classified as__________

A

ZWITTERIONS

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3
Q

-formed when the carboxyl group on one amino acid links to the amino group of another amino acid with the loss of a water molecule

A

PEPTIDE BOND

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4
Q

-End of protein structure with a free amino group

A

N-TERMINAL

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5
Q

-End of protein structure with a free carboxyl group

A

C-TERMINAL

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6
Q

-at low pH

A

CATION

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7
Q

-at high pH

A

ANION

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8
Q
  1. It helps to grow and repair body tissues
  2. Maintain the myelin sheaths that protect nerve cells
  3. Serves as the precursor for several hormones end
A

HISTIDINE

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9
Q

Branched chain amino acid group

A

ISOLEUCINE, LEUCINE, AND VALINE

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10
Q

-concentrated in muscle tissues and essential for wound healing, immune function, glucose hemostasis, and hemoglobin formation

A

ISOLEUCINE

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11
Q

-regulation of blood glucose, wound healing, and prevention of muscle protein degradation

A

LEUCINE

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12
Q

-promotes mental health and muscle coordination

A

VALINE

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13
Q
  1. Production of antibodies and maintaining healthy tissues
    2.Helps in the absorption and conservation of calcium
  2. Serves an important role in the formation of collagen
A

LYSINE

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14
Q
  1. helps to initiate the translation of messenger RNA, stabilizes protein structure, and important cellular antioxidant
  2. it is an important source of sulfur for normal metabolism and growth
  3. Assists in the breakdown of fats, and detoxifies lead and other heavy metals
  4. Helps to diminish muscle weakness and prevents brittle hair
A

METHIONINE

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15
Q
  1. metabolic precursor for tyrosine-essential for the production of dopamine horepinephrine, and epinephrine.
A

PHENYLALANINE

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16
Q
  1. Important component in the formation of collagen, elastin, and tooth enamel
  2. important production of neurotransmitters and overall health of the nervous system.
  3. Helps to maintain proper protein balance, aids liver function and metabolism of porphyrins
A

THREONINE

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17
Q
  1. Metabolic precursor for serotonin and melatonin which regulate appetite, mood, sleep, and pain
  2. Natural relaxant that helps alleviate insomnia, and soothes anxiety, and depression
  3. Essential for the production of niacin
A

TRYPTOPHAN

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18
Q
  1. Major role in the transfer of nitrogen from peripheral tissues to the liver for processing and excretion and strengthens the immune system by antibodies
  2. Serves as a source of energy for the central nervous system
  3. Helps in reducing the buildup of toxic substances released when muscle protein is broken down
A

ALANINE

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19
Q
  1. Plays an important role in the synthesis of ammonia
  2. The primary function is the conversion of one amino acid into another via amination or transamination
A

ASPARAGINE

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20
Q
  1. Serve as the precursor for several other amino acids, such as asparagine, arginine, lysine, methionine, threonine, and isoleucine
A

ASPARTIC ACID OR ASPARTATE

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21
Q
  1. Produced from the transamination of amino acids such as alanine and aspartic acid
  2. Serves as neurotransmitter and has important role in the metabolism of CHO and fats
A

GLUTAMIC ACID OR GLUTAMATE

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22
Q
  1. Unlike other amino acids, it is not directly coded in the genetic code, rather it is encoded to UGA codon.
  2. Only one synthesized on its tRNA in all domains of life
  3. Only amino acid containing an essential dietary micronutrient (selenium) as a constitutive component
A

SELENOCYSTEINE

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23
Q
  1. Need for the proper metabolism of lipids and fatty acids
  2. Plays an important role in the synthetic pathways of pyrimidines, purines, creatinine, and porphyrins serve as a component of the protective myeline sheaths surrounding nerve fibers
  3. Aids in the production of antibodies
A

SERINE

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24
Q
  1. Plays an important role in cell division, wound healing, stimulation of protein synthesis, immune function, and the release of hormone.
  2. Conversion of ammonia to urea
A

ARGININE

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25
1. Synthesized from glutamic acid with an addition of ammonium group and donate the ammonium group form urea 2. Renal maintenance of the acid-base balance, providing fuel for healthy digestive tract and basis of the building blocks for synthesis of RNA and DNA
GLUTAMINE
26
1. Potentially toxic so it is absorbed during digestion to convert into cystine-more stable in the G.I tract and less toxic 2. Important structural and functional component for proteins Found in beta-keratin and is important in collagen formation
CYSTEINE
27
1. Essential for synthesis of nucleic acids, proteins, peptides, purines, ATP, porphyrins, hemoglobin, glutathione, creatine, bile salts, glucose, glycogen, and other amino acids 2. Limits muscle degeneration, improves glycogen storage, promotes healing, detoxification in the liver.
GLYCINE
28
1. Produced from glutamic acid and other amino acids 2. Serves as precursor for hydroxyproline-manufactured in collagen, ligaments, and cardiac tissues, tendons. 3. Involves wound healing especially the cartilage, strengthening of joints, tendons, and cardiac tissues.
PROLINE
29
1. Serves as a precursor for adrenal and thyroid hormones. 2. Stimulates metabolism and the nervous system, acts as a mood elevator and aids in function of the adrenal, thyroid, and pituitary glands.
TYROSINE
30
Proteins comes from the greek word_________ meaningf "first rank of importance"
proteios
31
Large molecules referred to as:
MACROMOLECULES
32
Fundamental building block or protein:
AMINO ACIDS
33
Protein soluble in water is:
ALBUMIN
34
Element that distinguishes protein from CHO and Lipids is:
NITROGEN
35
participation as buffers to maintain pH
Acid-base balance
36
part of immune defense system
Antibodies
37
hormones and receptors
Hormones
38
connective tissue
Structure
39
catalyst
Enzymes
40
participation in coagulation of blood
Hemostasis
41
1. it is the linear sequence of the amino acids 2. Any change in the amino acid composition can significantly alter the protein
PRIMARY STRUCTURE
42
It involves the winding of the polypeptide chain
SECONDARY REACTION
43
1. It is the actual three-dimentional configuration; the folding pattern of proteins 2. It is responsible for many of the physical and chemical properties of proteins
TERTIARY STRUCTURE
44
It is the association of two or more polypeptide chains to form a functional protein molecule
QUATERNARY STRUCTURE
45
It is a balance between anabolism (synthesis) and catabolism (breakdown)
NITROGEN BALANCE
46
1. This happens when more nitrogen is incorporated in the body than excreted ex: pregnant women, growing children, and adults recovering from major illness
POSITIVE NITROGEN BALANCE
47
1. Happens when more nitrogen is excreted than is incorporated into the body ex: burns, wasting diseases, continual high fever, and starvation
NEGATIVE NITROGEN BALANCE
48
degrades extracellular proteins
LYSOSOMAL PATHWAY
49
degrades important intracellular proteins
CYTOSOLIC PATHWAY
50
central reaction that remove amino acid nitrogen from the body or removal of nitrogen from free amino acids
TRANSAMINATION
51
1. Removal of amine group from a molecule. Enzyme which catalyze this reaction are deaminases 2. In the human body, deaminaton takes place primarily in the liver, however glutamate is also deaminated in the kidneys
DEAMINATION
52
Form of amino acid with two differing charges and with a net charge of zero
ZWITTERION
53
The pH value at which the sum of a molecule's charges equals zero
ISOELECTRIC POINT
54
1. A term used to describe the loss of the native or naturally occuring folded structure of proteins.
DENATURATION
55
Types of Denaturation
1. HEAT 2. CHEMICAL 3. MECHANICAL
56
Contain peptide chains composed of amino acids linked by peptide bonds
SIMPLE PROTEINS
57
1. It migrates ahead of albumin 2. migrates most anodally (toward the positive pole) 3. It is used as a landmark to confirm that the specimen is CSF; it crosses more easily into the CSF rather than other proteins
PREALBUMIN/TRANSTHYRETIN
58
Method for measurement of prealbumin
Nephelometry
59
Reference range of prealbumin
18-45 mg/dl
60
1. It is the most abundant protein in plasma 2. It is a general transport protein and buffers pH and is negative acute-phase reactant protein 3. It maintains osmotic pressure 4. It is an indicator of nutritional status 5. Affects the half-life of drugs
ALBUMIN
61
Method for measurement of Albumin
Dye Methods
62
What is the two dye methods
bromcresol green and bromcresol purple
63
reference range of albumin
3.5-5.0 g/dl
64
severe manifestation of protein-energy malnutrition (PEM)
MARASMUS
65
-It is a group of proteins consisting of a1, a2, B, and y fractions - It is usually measured by subtracting the value of serum albumin from the total protein concentration.
Globulin
66
Method for measurement of Globulin
Indirect method
67
Reference range for globulin
2.3-3.5 g/dl
68
1. Acute ohase reactant 2. Protease inhibitor 3. 90% of a a1-globulin band 4. Inactivates trypsin and other proteolytic enzymes 5. The most abundant acute phase reactant
Alpha-1 antitrypsin
69
Reference Value for Alpha-1 antitrypsin
145-270 mg/dl
70
1. It is a glycoprotein that migrates between albumin and a-1 globulin band 2. It is the most abundant protein in fetal serum 3. It peaks in the fetus at 13 weeks of gestation 4. Serve as tumor marker
Alpha-1 fetoprotein
71
Reference Value for Alpha-1 fetoprotein
5ng/ml
72
1. AKA: Orosomucoid 2. A major plasma glycoprotein that is negatively charged 3. Produced by the liver 4. An acute phase reactant 5. Useful diagnostic tool in neonatal bacterial infection (NOT WIDELY USED)
Alpha-1 acid glycoprotein
73
Transports Lipids (HDL)
Alpha-1 Lipoprotein
74
1. Serine protease inhibitor 2. Binds and inactivates pancreatic elastase, mast cell, chymase, and chymotrypsin 3. Associated with the pathogenesis of Alzheimer's disease because it is an integral component of the amyloid deposits
Alpha-1 Antichymotrypsin
75
Reference Range for Alpha-1 Antichymotrypsin
30-60 mg/dl
76
Inhibits serine proteases
Inter-a-trypsin inhibitor
77
1. Produced by hepatocytes 2.Major carrier protein of Vitamin D 3. Transports Vitamin D and bind actin 4. Important in bone formation and immune system
Gc-Globulin/Group Specific component (Gc)
78
1. Synthesize by the hepatocytes 2. Evaluate hemolytic anemia 3. Binds free hemoglobin to prevent urinary loss 4. Useful marker for hemolysis and hemoglobinuria 5. Independent risk factor for CVD 6. Used for paternity testing
HAPTOGLOBIN
79
Reference Range for Haptoglobin
26-185 mg/dl
80
1. Copper-carrying protein with enzymatic activities 2. 90% of copper bound to ceruloplasmin 3. Marker for Wilson's disease
CERULOPLASMIN
81
Reference Value for Ceruloplasmin
18-45 mg/dl
82
1. Protease inhibitors, a variety of proteases like trypsin, thrombin, kallikrein and plasmin 2. Largest non-lg plasma protein (800,000 D) 3. Synthesized by the liver 4. A major component of A2-globulin fraction
Alpha 2-macroglobulin
83
Reference Value for Alpha 2-macroglobulin
18-45 mg/dl
84
1. Synthesized by the liver 2. 2 molecules of Ferric iron bind reversibly by preventing iron deposition in tissue 3. Amajor component of the beta globulin fraction 4. Negative Acute Phase Reactant
Transferrin (Siderophilin)
85
1. Natural defense and enhanced immune response by cell lysis 2. Synthesize by the liver
Complement
86
most abundant complement protein in human serum
C3
87
second most abundant
C4
88
Reference range for complement
30-75 U/ml
89
1. precursor of a fibrin clot, elevate with other acute phase reactants 2. one of the largest proteins in plasma 3. classified as a glycoprotein 4. normally seen between beta-gamma region in electrophoresis
Fibrinogen
90
Reference range for fibrinogen
200-400 mg/dl
91
1. Synthesized by the liver 2. A small beta globulin that binds to free heme 3. used to measure/diagnose hemolytic uremic syndrome 4. acute phase reactant
hemopexin
92
Transports lipids (VLDL)
Pre-B-lipoprotein
93
Transports lipids (LDL)
B-lipoprotein
94
Transports lipids (LDL)
B-lipoprotein
95
1. Single polypeptide chain that is a component of the light chain of HLA class I 2. Freely filtered by the glomerulus and completely reabsorbed
B2- microglobulin
96
1. APR promotes phagocytosis 2. Cardiac marker and inflammatory marker
C-reactive protein
97
glycoproteins produced by plasma B cells
Immunoglobulins
98
is most abundant antibody in plasma and lymph
IgG
99
is the main antibody in mucous secretion
IgA
100
is the first antibody that appears in response to antigenic stimulation
IgM
101
is the antibody for allergic and anaphylactic reactions
IgE
102
is present mostly on the surface of B cells
IgD
103
1. Type of cancer that develops from plasma cells in the bone marrow 2. Increased plasma cells 3. Elevated Total Protein 4. Elevated serum creatinine 5. Increased ionized calcium 6. Urine: (+ ) Bence Jones Protein 7. Electrophoretic pattern: Presence of a shape peak in the gamma globulin region
MULTIPLE MYELOMA
104
1. An autoimmune disorder in which the body attacks itself by mistake 2. Presence of oligoclonal banding 3. Demyelination 4. Increased myelin basic protein
MULTIPLE SCLEROSIS