Molecular Biology I Flashcards

0
Q

What is the extra- and intra-cellular concentrations (mM) of K+?

A

Extra: 3.5-5

Intra: ~150

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1
Q

What is the extra- and intra-cellular concentrations (mM) of Na+?

A

Extra: 135-150

Intra: ~15

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2
Q

What is the extra- and intra-cellular concentrations (mM) of Ca2+?

A

Extra: ~1.3

Intra: ~0.1 (or ~100microMolar)

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3
Q

What is the extra- and intra-cellular concentrations (mM) of Mg2+?

A

Extra: ~0.6

Intra: ~0.8

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4
Q

What is the extra- and intra-cellular concentrations (mM) of H+?

A

Extra: 35-45nM (pH = 7.35-7.45)

Intra: ~100nM (ph ~ 7)

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5
Q

What is the extra- and intra-cellular concentrations (mM) of Cl-?

A

Extra: 100-120

Intra: ~5 - ~80

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6
Q

What is the extra- and intra-cellular concentrations (mM) of HCO3-?

A

Extra: 22-27
Intra: ~10

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7
Q

What are the two major types of epithelial cells?

A

Stratified: mechanical protection (skin)
Simple: secretion and absorption (lungs)

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8
Q

Where is the epithelia specialized for exchange?

A

The lungs. 02 and CO2

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9
Q

Where is epithelia specialized for absorption?

A

The gut and kidneys.

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10
Q

How many cells are in our body?

A

37 trillion

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11
Q

What are two proteins used in proof reading?

A

EF-Tu and EF-G

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12
Q

When are the proofreading proteins used?

A
  1. EF-Tu comes in with the new tRNA and AA and make sure it fits into the A site of the ribosome.
  2. After chain has been elongated, EF-G comes in to make sure it’s all good. When A site is restored, EF-G gets kicked off.
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13
Q

What are the three sites in the ribosome? Function?

A
  1. A: where new tRNA comes in with new AA (when this happens, rRNA in E site gets kicked out.)
  2. P: where chain is actually elongated.
  3. E: exit chamber for no longer needed tRNA.
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14
Q

Does proofreading require energy?

A

Yes. GTP to GDP for use of both EF-Tu and EF-G.

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15
Q

What percent of the cell’s membrane is the plasma membrane?

A

About 5%.

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16
Q

How does transportation to the cell membrane change a protein?

A
  • often makes them active
  • lots of conformational changes as they enter the membrane.
  • bind with other proteins.
17
Q

What is the life cycle of a protein? (what can go wrong?)

A

i) Conception: Replication and Transcription (mutations)
ii) Birth: Translation (misincorporation, premature termination)
iii) Maturation: Folding (misfolding)
iv) Death: Degradation (accumulation)

18
Q

What determines a proteins 3D structure?

A

The 1D AA sequence. (however, sometimes the environment can influence it.)

19
Q

How is protein folding determined?

A

The protein moves towards a lower free energy, and that determines structure.

20
Q

Describe the analogy of a protein’s intermediate state.

A

UF protein is like an atom in gaseous state.
Intermediate protein is like an atom as a liquid, more structure but very mobile.
Folded proteins are like a crystal.

21
Q

Do most proteins have an intermediate state?

A

yes.

22
Q

Who does the ribosome give a new protein to?

A

Chaperone Proteins.

23
Q

What is the role of chaperones?

A

They facilitate the folding of proteins.

24
Q

When are proteins unfolded?

A
  1. translocation
  2. degradation
  3. post translation modification
  4. stress can unfold proteins.
25
Q

What are heat shock proteins?

A

Chaperone proteins.

26
Q

What are the 5 families of HSPs?

A
  1. sHSPs (small)
  2. HSP60
  3. HSP70
  4. HSP90
  5. HSP100
27
Q

What do sHSPs do?

A

Provide an alternate surface for mis/unfolded proteins to bind to so that the cell can deal with them more easily. Help refold misfolded proteins.

28
Q

What do HSP90s do?

A

fold steroid hormone receptors and oncogenic kinases.

29
Q

What does HSP100 do?

A

Disaggregate large aggregates.

30
Q

What does HSP70 do?

A

It works with HSP90 and HSP100. Binds to new proteins very early on as it leaves the ribosome.

31
Q

What do HSP60 do?

A

?

32
Q

What are the two major degradation pathways?

A
  1. Proteasomes

2. Autophagosomes

33
Q

What causes Cystic Fibrosis?

A

the CFTR protein does not fold properly, so it is degraded.

34
Q

What is a prion?

A

A misfolded protein that can cause other of the same type of proteins to also become misfolded. It is infectious and the cause of Mad Cow’s Disease.

35
Q

What are epithelium?

A
  • avascular tissue, covers exterior body and closed cavities
  • polar: apical, basal and lateral
  • cell junctions: adherents, tights junctions, desmosomes
  • basal lamina
  • microvilli, cilia, other special appendages
36
Q

What are two classifications of epithelia?

A
  1. Layers: simple, stratified, pseudo-stratified

2. Shape: squamous, cuboidal, columnar

37
Q

What are 2 types of epithelia?

A
  1. Endothelium: lines lumen of blood vessels

2. Mesothelium: lines all cavities of the body and surfaces of abdominal organs.

38
Q

Flux is proportional to?

A

R squared

39
Q

Concentration is proportional to?

A

1/r