Week 2 Richter ILA's Flashcards

1
Q

proteins that use highly frequent codons get expressed at what rate

A

a higher rate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

this translocation mutation causes leukemia

A

chromsome 22 to 9

Philadelphia chromosome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

mutation that does not change function of protein

A

silent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

mutation that changes function of protein

A

missense

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

mutation that causes termination of protein

A

nonsense

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Purines

A

A and G

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Pyrimidines

A

C, U, T

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

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

A

CF (cystic fibrosis)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

amino acid sequence makes up what structure

A

primary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

alpha helix
beta sheet

A

secondary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

alpha helix and beta sheets together

A

tertiary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

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

A

quaternary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

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

A

peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

most important structural motif in proteins

A

alpha helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

which amino acids prefer helix

A

MALEK

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

what bonding is important for alpha helix

A

intra-chain H bonding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
Q

infectious agent that cause misfolding of the normal form of the protein (PrPc)

A

Prion proteins (PrPSc)

25
Q

oxygen saturated Hb

A

in the lungs

26
Q

oxygen free Hb

A

in the tissues
(Hb gives off oxygen to myoglobin in tissues and myoglobin will bind until it is time to contract muscle)

27
Q

oxygen saturation curve for myoglobin is left shifted: what does that mean?

A

higher affinity than hemoglobin

28
Q

oxygen saturation curve for hemoglobin is sigmoidal: why

A

sigmoidal suggests cooperativity b/t subunits (the more O2 that binds, increases O2 affinity)

29
Q

when pH lowers, where does oxygen saturation curve shift

A

to the right

(less affinity means hemoglobin will give off O2 easier, and thats what you want to happen in tissues)

30
Q

what will increased 2,3-BPG do to curve

A

shift to the right

(blood from individuals adapted to high altitudes-more glycolysis and less affinity for O2 so it can be released)

31
Q

main affect of carbon monoxide on oxygen saturation curve

A

occupies Hb and prevents O2 from binding (total capacity of O2 is reduced vertically)

32
Q

predominant form of Hb

A

HbA

33
Q

form of Hb induced by sickle cell anemia

A

HbF

34
Q

form of Hb induced by thalassemias

A

HbA2

35
Q

form of Hb increased in diabetics; proportional to blood glucose in the body

A

HbA1c

36
Q

extracellular fibrous proteins

A

collagen and elastin

37
Q

main part of collagen structure

A

alpha chain

(quaternary structure-3 chains linked together)

38
Q

cleavage of N and C terminus of procollagen happens where

A

extracellular space

39
Q

striated look of collagen is simply the what

A

collagen fibril regions

40
Q
A