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Pathophysiology > Proteins (Exam 3) > Flashcards

Proteins (Exam 3) Flashcards

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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
protein misfolding is the basis for
numerous human diseases
25
osmolytes
small compounds that enhance proper protein folding result into native folded functional species
26
how do osmolytes induce folding?
solvophobic effects of the peptide backbone
27
primary structure of protein
amino acid chain
28
secondary structure of protein
alpha helix chain, beta sheet
29
tertiary structure of protein
domain/subunits
30
hemoglobin is an example of
quaternary structure
31
proteome
large amount of functional proteins (one protein may have many functions)
32
large proteome is due to
post translational modifications
33
phosphorylation of a protein can provide for
different kinds of conformations
34
3 main therapeutic approaches to avoid misfolding
inhibition of protein aggregation interference with post translational peptide changes before misfolding up regulation of molecular chaperones/aggregate clearance mechanisms
35
functional plasma enzymes
known functions present in the blood
36
non functional plasma enzymes
no known functions absent for blood
37
sources of nonfunctional plasma enzymes
increase in rate of enzyme synthesis obstruction of normal pathway increased permeability of membrane cell damage and release of its contents
38
tissue damage or necrosis increases the levels of
several nonfunctional enzymes
39
measurement of nonfunctional plasma enzymes is important for
diagnosis of diseases prognosis of diseases
40
what two enzymes are important for the diagnosis of liver disease
alanine transaminase aspartate transaminase
41
which enzyme is more specific for the diagnosis of liver disease? why?
alanine transaminase plasma concentration increases ONLY in liver diseases
42
Aspartate transaminase is expressed in
a variety of tissues liver, brain, pancreas, heart, kidneys, lungs and skeletal muscles
43
does increased AST levels mean there is always tissue injury in the liver?
NO
44
does increased ALT levels mean there is always tissue injury in the liver?
YES
45
AST/ALT ratio less than one
non alcoholic fatty liver disease
46
AST/ALT ratio equal to one
acute viral hepatitis or drug related liver toxicity
47
AST/ALT ratio higher than one
cirrhosis
48
AST/ALT ratio higher than 2:1
alcoholic liver disease
49
when there is extremely high levels of alkaline phosphatase enzyme
obstructive liver diseases
50
when there is increased AST and ALT and EXTREMELY high levels of ALP
obstructive jaundice
51
when there is EXTREMELY high levels of AST and ALT and high levels of ALP
hepatitis
52
isoenzymes
different forms of an enzyme that catalyze the same reaction in different cells/tissues
53
isoenzymes have _____________ structure with _________________
quaternary structures slight variations in aa
54
LDH1 location and importance
heart, RBC myocardial infarction
55
LDH2 location and importance
white cells megaloblastic anemia, leukemia, malignancy
56
LDH3 location and importance
lung pulmonary infarction
57
LDH4 location and importance
kidney, placenta, pancreas kidney/pancreatic disease
58
LDH5 location and importance
liver, skeletal muscle liver disease, muscle injury
59
CK-MD (cardiac enzyme)
biomarker of myocardial infarction
60
myocardial infarction may be indicated by
an increase in the levels of creatine kinase and lactate dehydrogenase
61
what do a majority of drugs target?
proteins duh!
62
proteins as therapeutic tools
stability intracellular delivery desirable pharmacokinetics desirable pharmacodynamics
63
why proteins against small drug molecules?
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
protein vaccines
protecting against a deleterious foreign agent treating an autoimmune disease treating cancer
65
protein therapeutics with specific targeting activity
interfering with a molecule/organism delivering other compounds/proteins
66
protein therapeutics with enzymes/regulatory activity
replacing a protein that is deficient/abnormal augmenting an existing pathway providing a novel function
67
example of replacing a protein that is deficient or abnormal
insulin therapy
68
rapid acting insulin
taken right before eating lower high blood glucose level
69
short acting insulin
taken right before eating lower high blood glucose level
70
intermediate acting insulin
taken at bedtime or BID
71
extended long acting
taken once or twice a day
72
premixed insulin
time taken depends on the combination
73
at physiological conditions, insulin molecules exist in the
monomeric form

Pathophysiology (18 decks)

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