Week 2 Richter ILA's Flashcards

(41 cards)

1
Q

proteins that use highly frequent codons get expressed at what rate

A

a higher rate

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2
Q

this translocation mutation causes leukemia

A

chromsome 22 to 9

Philadelphia chromosome

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3
Q

mutation that does not change function of protein

A

silent

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4
Q

mutation that changes function of protein

A

missense

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5
Q

mutation that causes termination of protein

A

nonsense

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6
Q

Purines

A

A and G

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7
Q

Pyrimidines

A

C, U, T

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8
Q

example of missense mutation where there is a deletion of 508 on CFTR gene

A

CF (cystic fibrosis)

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9
Q

amino acid sequence makes up what structure

A

primary

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10
Q

alpha helix
beta sheet

A

secondary

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11
Q

alpha helix and beta sheets together

A

tertiary

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12
Q

multiple amino acid chains assembled together (2 alpha helix and beta sheets)

A

quaternary

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13
Q

partial double bond
rigid, planar
trans-configuration
uncharged; polar

A

peptide bond

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14
Q

most important structural motif in proteins

A

alpha helix

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15
Q

which amino acids prefer helix

A

MALEK

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16
Q

what bonding is important for alpha helix

A

intra-chain H bonding

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17
Q

what bonding is important for beta sheets

A

interchain H bonding

18
Q

which amino acids are found in beta sheets

A

aromomatic residues
(tyr, phe, trp)

19
Q

what bonding is important for tertiary structure

A

H bonding of side chains

20
Q

transcription factor that is a homodimer and held together by hydrophobic faces of parallel Leu zippers

A

Leu zipper (bZIP)

21
Q

transcription factor that has its domain in MyoD (essential for muscle development)

A

bHLH (basic helix-loop-helix)

22
Q

calcium binding happens in the loop region of what motif

A

helix-loop-helix

22
Q

example of beta barrel

A

porins (antibiotics)

23
Q

happens from accumulation of misfolded proteins (plaques of Tau); amyloid abeta

A

Alzheimer’s disease

24
infectious agent that cause misfolding of the normal form of the protein (PrPc)
Prion proteins (PrPSc)
25
oxygen saturated Hb
in the lungs
26
oxygen free Hb
in the tissues (Hb gives off oxygen to myoglobin in tissues and myoglobin will bind until it is time to contract muscle)
27
oxygen saturation curve for myoglobin is left shifted: what does that mean?
higher affinity than hemoglobin
28
oxygen saturation curve for hemoglobin is sigmoidal: why
sigmoidal suggests cooperativity b/t subunits (the more O2 that binds, increases O2 affinity)
29
when pH lowers, where does oxygen saturation curve shift
to the right (less affinity means hemoglobin will give off O2 easier, and thats what you want to happen in tissues)
30
what will increased 2,3-BPG do to curve
shift to the right (blood from individuals adapted to high altitudes-more glycolysis and less affinity for O2 so it can be released)
31
main affect of carbon monoxide on oxygen saturation curve
occupies Hb and prevents O2 from binding (total capacity of O2 is reduced vertically)
32
predominant form of Hb
HbA
33
form of Hb induced by sickle cell anemia
HbF
34
form of Hb induced by thalassemias
HbA2
35
form of Hb increased in diabetics; proportional to blood glucose in the body
HbA1c
36
extracellular fibrous proteins
collagen and elastin
37
main part of collagen structure
alpha chain (quaternary structure-3 chains linked together)
38
cleavage of N and C terminus of procollagen happens where
extracellular space
39
striated look of collagen is simply the what
collagen fibril regions
40