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Pathophysiology > Proteins (Exam 3) > Flashcards

Proteins (Exam 3) Flashcards

1
Q

Proteins are the most

A

diverse group of biologically important substances

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1
Q

Proteins

A

Organic compounds that contain nitrogen, carbon, hydrogen, and oxygen

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2
Q

Building block of life?

A

Proteins
Necessary for building and repair of body tissues

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3
Q

Proteins produce

A

Enzymes, receptors, hormones

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4
Q

What are proteins made of?

A

Amino acids

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5
Q

Each protein needs to have

A

Stability and comfortability

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6
Q

Where does protein transcription happen?

A

Nucleus

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7
Q

protein translation

A

occurs in Cytosol
requires charges tRNA and ribosome
one reading frame
codons

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8
Q

codon

A

5 to 3
DNA/RNA sequence of three nucleotides
64 different codons

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9
Q

anticodon

A

3 to 5
trinucleotide sequence located at one end of tRNA
complementary to corresponding codon

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10
Q

codon wobble

A

tRNA codon can recognize more than one codon
atypical base pairing in third position of codon

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11
Q

wobble hypothesis

A

first two codons pair precisely, the third bases may wobble

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12
Q

the wobble hypothesis allows mRNA to be

A

translated with fewer tRNAs than would be required without wobble

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13
Q

does transcription/translation occur simultaneously in prokaryotes? eukaryotes?

A

prokaryotes - yes

eukaryotes - no

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14
Q

mRNAs of bacteria are ________ while eukaryote mRNAs are ___________

A

polycistronic (several sites for initiating/terminating)

monocistronic

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15
Q

acceptor arm of tRNA

A

attachment of amino acid

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16
Q

anticodon loop of tRNA

A

interacts with mRNA

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17
Q

tRNA

A

adaptor molecule composed of RNA
76-90 nt
link between mRNA and aa sequence of proteins

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18
Q

tRNA synthetase

A

charges tRNA
specific for an amino acid

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19
Q

structures of ribosomes in prokaryotes vs eukaryotes

A

pro - 70S
eu - 80S

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20
Q

release factor protein

A

binds at the stop codon
signals end of translation, breaks ribosome/mRNA complex

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21
Q

protein folding

A

process by which polypeptide chain gets its 3D structure to achieve its active state

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22
Q

consequences of amyloid fibril formation

A

alzheimers
huntingtons
prion disease
diabetes type 2
parkinsons

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23
Q

what does ubiquitin proteasome system do to misfolded proteins?

A

degrades proteins to avoid cytotoxicity

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24
Q

protein misfolding is the basis for

A

numerous human diseases

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25
Q

osmolytes

A

small compounds that enhance proper protein folding
result into native folded functional species

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26
Q

how do osmolytes induce folding?

A

solvophobic effects of the peptide backbone

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27
Q

primary structure of protein

A

amino acid chain

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28
Q

secondary structure of protein

A

alpha helix chain, beta sheet

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29
Q

tertiary structure of protein

A

domain/subunits

30
Q

hemoglobin is an example of

A

quaternary structure

31
Q

proteome

A

large amount of functional proteins (one protein may have many functions)

32
Q

large proteome is due to

A

post translational modifications

33
Q

phosphorylation of a protein can provide for

A

different kinds of conformations

34
Q

3 main therapeutic approaches to avoid misfolding

A

inhibition of protein aggregation
interference with post translational peptide changes before misfolding
up regulation of molecular chaperones/aggregate clearance mechanisms

35
Q

functional plasma enzymes

A

known functions
present in the blood

36
Q

non functional plasma enzymes

A

no known functions
absent for blood

37
Q

sources of nonfunctional plasma enzymes

A

increase in rate of enzyme synthesis
obstruction of normal pathway
increased permeability of membrane
cell damage and release of its contents

38
Q

tissue damage or necrosis increases the levels of

A

several nonfunctional enzymes

39
Q

measurement of nonfunctional plasma enzymes is important for

A

diagnosis of diseases

prognosis of diseases

40
Q

what two enzymes are important for the diagnosis of liver disease

A

alanine transaminase
aspartate transaminase

41
Q

which enzyme is more specific for the diagnosis of liver disease?

why?

A

alanine transaminase

plasma concentration increases ONLY in liver diseases

42
Q

Aspartate transaminase is expressed in

A

a variety of tissues

liver, brain, pancreas, heart, kidneys, lungs and skeletal muscles

43
Q

does increased AST levels mean there is always tissue injury in the liver?

A

NO

44
Q

does increased ALT levels mean there is always tissue injury in the liver?

A

YES

45
Q

AST/ALT ratio less than one

A

non alcoholic fatty liver disease

46
Q

AST/ALT ratio equal to one

A

acute viral hepatitis or drug related liver toxicity

47
Q

AST/ALT ratio higher than one

A

cirrhosis

48
Q

AST/ALT ratio higher than 2:1

A

alcoholic liver disease

49
Q

when there is extremely high levels of alkaline phosphatase enzyme

A

obstructive liver diseases

50
Q

when there is increased AST and ALT and EXTREMELY high levels of ALP

A

obstructive jaundice

51
Q

when there is EXTREMELY high levels of AST and ALT and high levels of ALP

A

hepatitis

52
Q

isoenzymes

A

different forms of an enzyme that catalyze the same reaction in different cells/tissues

53
Q

isoenzymes have _____________ structure with _________________

A

quaternary structures

slight variations in aa

54
Q

LDH1 location and importance

A

heart, RBC

myocardial infarction

55
Q

LDH2 location and importance

A

white cells

megaloblastic anemia, leukemia, malignancy

56
Q

LDH3 location and importance

A

lung

pulmonary infarction

57
Q

LDH4 location and importance

A

kidney, placenta, pancreas

kidney/pancreatic disease

58
Q

LDH5 location and importance

A

liver, skeletal muscle

liver disease, muscle injury

59
Q

CK-MD (cardiac enzyme)

A

biomarker of myocardial infarction

60
Q

myocardial infarction may be indicated by

A

an increase in the levels of creatine kinase and lactate dehydrogenase

61
Q

what do a majority of drugs target?

A

proteins duh!

62
Q

proteins as therapeutic tools

A

stability
intracellular delivery
desirable pharmacokinetics
desirable pharmacodynamics

63
Q

why proteins against small drug molecules?

A

diversity of functional groups
highly specific function - no mimicry
less interaction with normal processes
well tolerated due to being naturally produced in the body

64
Q

protein vaccines

A

protecting against a deleterious foreign agent
treating an autoimmune disease
treating cancer

65
Q

protein therapeutics with specific targeting activity

A

interfering with a molecule/organism
delivering other compounds/proteins

66
Q

protein therapeutics with enzymes/regulatory activity

A

replacing a protein that is deficient/abnormal
augmenting an existing pathway
providing a novel function

67
Q

example of replacing a protein that is deficient or abnormal

A

insulin therapy

68
Q

rapid acting insulin

A

taken right before eating

lower high blood glucose level

69
Q

short acting insulin

A

taken right before eating

lower high blood glucose level

70
Q

intermediate acting insulin

A

taken at bedtime or BID

71
Q

extended long acting

A

taken once or twice a day

72
Q

premixed insulin

A

time taken depends on the combination

73
Q

at physiological conditions, insulin molecules exist in the

A

monomeric form

Pathophysiology (15 decks)

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