C11 Amino Acids & Proteins Flashcards

(70 cards)

1
Q

Proteins

A

single most important group of organic compounds associated with living organisms

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2
Q

Lipids

A

water insoluble fatty molecules- require proteins in order to be transported through the plasma…lipoproteins

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3
Q

Amino acids

A

building blocks of proteins

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4
Q

DNA

A

very large molecule that contains biochemical codes to make proteins from amino acids

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5
Q

Genomics

A

study of DNA

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6
Q

Genome

A

all the DNA in a living organism

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7
Q

Nucleotides

A

2 purine bases (adenine and guanine)

2 pyrimidine bases (cytosine & thymine)

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8
Q

Adenine bonds with?

A

Thymine

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9
Q

Guanine bonds with?

A

Cytosine

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10
Q

Three groups of consecutive bases that provide the code for an amino acid?

A

codon

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11
Q

Sequence of DNA that provides the code for an entire protein?

A

Gene

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12
Q

When cells divide, the DNA condenses in visible structures called?

A

chromosomes

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13
Q

Each nucleated cell has 23 pairs of chromosomes, each representing a pair of DNA molecules which are joined at a central?

A

centromere

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14
Q

Human DNA contains how many genes?

A

20-25,000

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15
Q

DNA provides a code for the creation of?

A

mRNA

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16
Q

How is mRNA created?

A

actions of RNA polymerase and a promoter protein (Transcription)

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17
Q

What is translation?

A

When mRNA goes into the ribosomes where it meets up with individual amino acids and assembles them together to create proteins

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18
Q

What are DNA or NAT probes?

A

lab techniques that allow for the detection of specific nucleotide sequences

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19
Q

Advantages of DNA probes and NAT?

A

extremely specific, sensitive, and faster than routine culture

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20
Q

Disadvantages of DNA probes and NAT?

A

extreme sensitivity can cause problems if contaminated with outside sources, difficult and expensive techniques

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21
Q

All proteins are composed of?

A

amino acids

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22
Q

How many naturally occurring amino acids are there?

A

20

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23
Q

Aminoacidopathies?

A

uncommon, inherited, genetic disorders of amino acid metabolism

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24
Q

Most common aminoacidopathy?

A

Phenylketonuria (PKU)

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25
Phenylketonuria
autosomal recessive (requires 2 defective genes from both parents), absence of phenylalanine hydroxylase... si cannot be converted to tyrosine, it accumulates and is converted to phenylpyruvic acid (which is toxic to newborns and kids resulting in brain damage and mental retardation) damage begins 2-3 wks after birth, treated with dietary restrictions
26
Guthrie Test
Small disk of filter (PKU) paper is punched out and placed on agar plate containing Bacillus subtillis & B2 thienylalanine, the agar gel is able support bacterial growth but B2 thienylalanine inhibits it, though with extra phenylalanine bacteria can grow, growth is proportional to amount of phenylalanine in serum
27
Primary (Protein conformation)
amino acid sequence
28
Secondary (protein conformation)
winding, twisting of the amino acid chain, regulated by hydrogen bonding between different locations on the chain
29
Tertiary (protein conformation)
3D structure of the amino acid chain, regulated by chemical interactions between the "R" groups
30
Quaternary (protein conformation)
non-covalent bonding between 2 or more polypeptide chains
31
Amino acids are linked together by a special type of chemical bond called?
peptide bond
32
A peptide bond occurs between a __ and a ___ of another?
carboxyl group of one amino acid, amino group
33
Whenever 2 amino acids are linked together with a peptide bond, what molecule is produced?
water
34
amphoteric
may have a + or - electric charge
35
Most proteins are synthesized in?
the liver
36
Immunoglobulins are synthesized in?
B-lymphs
37
3 sources of amino acids?
digestion and absorption, synthesis by liver, and re-utilization from protein catabolism
38
How many of the 20 amino acids can be synthesized by the liver and how many must be ingested?
11 are synthesized, 9 must be ingested
39
Peptide chains composed only of amino acids?
simple proteins
40
composed of a protein fraction and a non protein fraction?
conjugated proteins
41
lipoproteins
protein+lipid
42
glycoprotein
protein+carbohydrate
43
nucleoprotein
protein+nucleic acids
44
General functions of proteins:
energy source, contribute to osmotic pressure, act as buffers, transport molecules, coagulation/hemostasis, immune function, hormones and hormone receptors, structural molecules
45
Prealbumin
migrates ahead of albumin, decreased amt indicated poor nutrition, 15-40 mg/dl
46
Albumin
highest concentration of proteins, 80% of tissue osmotic pressure, major transport and binding protein, decreased amt associated with poor nutrition, liver, and renal disease
47
Alpha-1-Anti-Trypsin
Migrates in Alpha1 band, acute phase reactant, decreased amt associated with pulmonary disease
48
Alpha-1-Fetoprotein
Migrates between alpha1 and albumin band, synthesized in yolk sac and liver during gestation decreases after birth, increased: spina bifida, neural tube defects, twins, hepatocellular cancer, decreased: down syndrome and trisomy 18
49
Haptoglobin
Alpha 2, binds free hemoglobin, preventing loss in urine,, increased: inflammatory conditions, decreased: intravascular hemolysis
50
Transferrin
Beta, iron transport protein, increased with iron deficiency, decreased with anemia
51
Hemopexin
beta, acute phase reactant, bind free heme and transports it to liver
52
Complement
activated can lyse cells, C3 and C4 most abundant, increased in acute inflammatory conditions, decreased in chronic autoimmune disorders (RA and LE)
53
C-Reactive Protein (CRP)
Gamma, increased in infection, gout, autoimmune disease, cancers, tissue necrosis, early indicator for CVD and Type 2 diabetes
54
hs-CRP (high sensitivity)
high CRP in lower survival post AMI and arterial re-closure post balloon angioplasty,
55
Immunoglobulins
gamma, each antibody has 2 heavy & 2 light chains, antibody specificity determined by variable region at end of heavy & light chains, light chains are kappy lambda, multiple myeloma produces large concentrations of a single class of IgG, Waldenstrom's disease produces IgM
56
IgG
increased in chronic infections
57
IgM
increased with acute infections
58
IgE
associated with parasitic infections & allergic immune reactions
59
IgA
found in secretions
60
Myoglobin
heme protein found in skeletal & cardiac muscle, AMI, elevated 1-3hrs post AMI, peaks at 5-12hrs post AMI, returns to normal by 18-30hrs, also elevated in crush injuries & renal failure 30-90ng/ml
61
Troponin
complex of 3 proteins that regulate muscle contraction in cardiac & skeletal muscle, associated with cardiac tissue & is useful to evaluate possible AMIs, elevated 3-4hrs post AMI, peaks 10-24hrs post AMI, remains elevated 10-14 days, single best test for the diagnosis of AMI <.06ng/ml
62
B-Type Natriuretic Peptide (BNP)
hormone the heart releases in response to increased heart pressure associated with CHF, increased BNP causes arterial and venous vasodilation, suppression of aldosterone and promotes diuresis (decreases bp) 0-100pg/ml
63
Actue Phase Proteins (Reactants)
Positive-increased concentration during inflammation | Negative-decreased concentration during inflammation
64
Hypoprotenemia
below normal TP indicates a negative nitrogen balance, decreased protein synthesis, increased protein loss
65
Hyperprotenemia
excessive protein synthesis, dehydration
66
Kjedahl Method for Total Protein
classic reference method used to standardize all other techniques (technically difficult, labor intensive, and expensive) based upon measurement of total nitrogen and the following relationship between nitrogen and protein (16%)(Total Nitrogen)=(Total Protein) No longer done routinely!
67
Biuret Method for Total Protein
**** most common technique, all proteins have peptide bonds, cupric ions react with peptide bonds to produce a violet color that is measured at 540 nm
68
Dry binding technique
most protein will bind with various dyes to produce colored complexes, downside is that different proteins have different affinities for different dyes resulting in variable results
69
Albumin determination
measured by Brom Cresol Green (BCG) and Brom Cresol Purple (BCP)
70
Refractometer
protein (and other substances) in solution refract light rays as they pass through the solution