Exam 1 Random Flashcards

1
Q

What nucleotide can be deaminated?

A

guanine -must be removed

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2
Q

RNA polymerase is a?

A

DNA directed RNA polymerase

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3
Q

RNA Guanine capping is in what direction?

A

5’-5’ linkage instead of 5’-3’

— stabilizes and protects from phosphates and nucleases

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4
Q

TF2H is a multiprotein that?

A

includes XPB (bubble) and XPD (encounters base)
unwinds DNA at transcription start site
unwinds DNA at the site of damage
contain two proteins that if one is mutated, causes xeroderma pigmentation (XPA)

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5
Q

etoposide

A

is a drug that targets the proteins (gyrase and topoisomerases) that detangle super-coils

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6
Q

sickle cell anemia arises due to?

A

insolubility of hemoglobin due to a point mutation in primary structure affecting beta subunit

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7
Q

chloramphenicol

A

inhibits protein synthesis by interfering with peptide bonds

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8
Q

human genome composed of how many nucleotides?

A

3.2x10^9 (3.2billion)

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9
Q

Shelterin complex

A

protect telomeres from DNA repair mechanisms, regulate telomerase activity. Consists of double- and single-stranded TTAGGG repeats and a single-stranded, G-rich overhang.

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10
Q

Cordycepin

A

RNA transciption inhibitor

looks like 3’deoxyadenosine

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11
Q

deoxyribose sugar plus a base is called?

A

nucleoside

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12
Q

Pentose + base + PO4-

A

nucleotide

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13
Q

template strand pairs with?

A

coding strand, mRNA strand, nascent DNA strand during DNA replication

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14
Q

What AA is achiral?

A

glycine

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15
Q

which AA are not used to assemble proteins in human cells?

A

D-amino

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16
Q

alpha helix is stabolized by?

A

H-bonds between every 4th AA

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17
Q

condition(s) resulting in reduced beta hemoglobin subunit

A

thalassemia major, beta-thallasemia, cooley anemia

18
Q

binding of a substrate to an enzymatic active site is primarily dependent on?

A

multiple weak interactions (like H-bonds)

19
Q

catalytic triad?

A

histidine, aspartate, serine

20
Q

Name AA that can be phosphorylated?

A

Tyrosine, serine, threonine

21
Q

difference between kinases and phosphatase?

A
  • kinases= add phosphate to Tyrosine, serine, threonine

* phosphatases= remove phosphoryl group from Tyrosine, serine, threonine

22
Q

is myoglobin allosterically regulated?

A

NO. But hemoglobin is, 23BPG is an allosteric regulator (more 23BPG to heme, lower O2 affinity)

23
Q

when oxygen binds to hemoglobin, what happens?

A

O coordinates the iron atom in the heme prosthetic group, iron atom in heme moves into the plane of protoporphyin, histidine side chain is pulled closer to heme

24
Q

hydrolytic deaminations cause cytosine to be converted into?

A

uracil

25
Q

why does replication and transcription occur in 5’-3’ direction?

A

it would work 3’-5’ direction until proofreading removed a nucleotide… so it needs to be 5’-3’ so we have a mechanism of proofreading

26
Q

reverse transcriptase is a?

A

RNA directed DNA polymerase

27
Q

What gives DNA strand polarity?

A

the way base pairs are linked (pentose sugar linkages give a charge)

28
Q

6 common steps in DNA processing?

A

site recognition, helicase, SSB, Nuclease, polymerase. ligase

29
Q

proteins produced in human cells are comprised exclusively of?

A

L-amino acids

30
Q

What AA is very like collagen?

A

glycine

31
Q

What makes methionine and cysteine special?

A

They both have “S” in their side chains

32
Q

AA zwitterion example?

A

alanine (increase pH= decrease H= deprotinates; lower pH=increase H= protinated)

33
Q

What is a proenzyme?

A

an enzyme containing its reqired prothetic group or cofactor (Ex: holoenzyme)

34
Q

What bonds contribute to 3rd structure?

A

H-bonds, ionic, disulfide, hydrophobic

35
Q

What antibiotic acts by blocking the tRNA binding to the A-site in the ribosome?

A

tetracycline

36
Q

What AA are in histones? Also in SSB?

A

Lysine and Arginine (bc they have a + charge)

37
Q

Catalytic tetramer moves stuff into?

A

peroxisomes

38
Q

TOM complex and transolcons?

A

Move stuff into the ER or the ER membrane

39
Q

Zellweger Syndrome

A

mutation, “empty peroxisomes”

40
Q

isozyme

A

similar enzymes/AA sequence that catalyze the same reaction (but typically under different conditions and different regulators)
o *point: catalyze same reactant and have similar AA