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BIO 041 > Chapter 4 > Flashcards

Chapter 4 Flashcards

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Biology 101 flashcards
1
Q

What is Kinesin?

A

motor protein, transports cellular cargo like organelles

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2
Q

What determines the function of a protein?

A

it’s shape

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3
Q

What is a primary structure? (1’)

A

linear sequence of amino acids

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4
Q

What holds together a primary structure?

A

peptide bonds hold together the linear AA’s

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5
Q

What is a secondary structure? (2’)

A

They are alpha helixes and beta strands

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6
Q

What holds together a secondary structure?

A

H-Bonds in the backbone of AA’s

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7
Q

What is a tertiary structure? (3’)

A

it is a 3D structure of a polypeptide

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8
Q

Other characteristics of the tertiary structure?

A
  • 1 protein and 1 polypeptide
  • H-bonds, Hydrophobic bonds, Van Der Waals, and polar/ non-polar bonds hold this together
  • all of secondary elements come together
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9
Q

What is a Quaternary Structure? (4’)

A

It is the same as a tertiary structure but it has 2 or more polypeptides

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10
Q

What is the shape of an alpha helix?

A

It is helix/ spiral shaped

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11
Q

what is the shape of a beta-strand?

A

Shaped like an arrow

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12
Q

What type of bond does protein folding depend on?

A

weak non-covalent bonds

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13
Q

Where are the hydrophobic bonds on the folded protein?

A

Inside

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14
Q

Where are the non-hydrophobic bonds? (hydrophilic)

A

Outside

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15
Q

What is a homodimer?

A

The same peptide twice

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16
Q

What is responsible for denaturing (unfolding) proteins?

A
  • Urea
  • Change in PH or Heat
  • Noncovalent bonds break first
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17
Q

What happens when the urea is removed?

A

The protein refolds into it’s original conformation

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18
Q

What is the native state of a protein?

A

full biological activity

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19
Q

What do chaperones do?

A

chaperones help proteins fold in the cell

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20
Q

What happens if chaperones are absent?

A

Proteins won’t have biological activity (which could lead to disease)

21
Q

What would happen to a protein without chaperones?

A

They would fold incorrectly

22
Q

One example of a disease caused by misfolded proteins

A

Mad Cow Disease (Bovine SPongiform encephalopathy) which is an infectious neurodegenerative disease

23
Q

What causes Alzheimer’s Disease

A

plaques in brain amyloid beta protein aggregation

24
Q

Where do H-bonds occur in an alpha helix?

A

They make up the back-bone and occur every 4 amino acids

25
Q

What proteins have the propensity to form an alpha helix?

A

M.A.L.E.K

26
Q

What makes up the backbone of the beta-sheet?

A

H-bonds

27
Q

What are the two types of beta sheets?

A

Parallel and Antiparallel

28
Q

What proteins have the propensity to form beta sheets?

A

W.I.F.T.Y.V.

29
Q

What are Amphipathic Motifs?

A

They are coils comprised of Hydrophobic and Hydrophilic components

30
Q

Where are Amphipathics Motifs found?

A

proteins are commonly found within the lipid bilayer

31
Q

What is a protein domain?

A

any segment of a polypeptide that can fold independently

32
Q

Factors for Binding site compatibility

A

-Size
-Shape
-Specific Interactions

33
Q

What do Enzymes do?

A

catalyze reactions

34
Q

How do Enzymes catalyze reactions?

A
  • Orients two substrate molecules
  • Rearrange charges in substrate
  • changes shape of substrate
35
Q

What is a Ligand?

A

Any substance bound by a protein

36
Q

What is another way to describe drugs (medicine)?

A

They are Ligands

37
Q

What causes Chronic myelogenous leukemia?

A

reciprocal translocation of chromosomes 9 and 22 (this speeds up cell division and prevents DNA repair)

38
Q

What is Linade and what does it do?

A

It is a Phosphorphorylate, it turns on mechanisms

39
Q

Why are some patients immune to the effects of Gleevec?

A

Random mutations in the BCR-Abl protein

40
Q

What is Nilotinib?

A

It is a second-generation CML drug, created by binding the Gleevec structure to the Abl Kinase domain.

41
Q

What does the positive track look like?

A

A makes B, then B makes C.
A -> B -> C

42
Q

What does Negative feedback look like?

A

A makes B which makes X, when too much of X is created, the Feedback Inhibitor stops X from being produced.

43
Q

What is Allosteric Regulation?

A

The regulatory molecule binds to sites other than the active site (induces conformational change)

44
Q

What is the role of ADP in Allosteric Regulation?

A

It is needed so the sugar can bind effectively to the Alosteric site.

45
Q

What does Protein Kinase do during phosphorylation?

A

Adds a phosphate group and it turns protein on

46
Q

What does protein Phosphatase do during Phosphorylation?

A

It removes the phosphate and turns protein off.

47
Q

DO eukaryotes have a five prime cap?

A

yes

48
Q

do prokaryotes have a five prime cap?

A

no they have an RBS

BIO 041 (12 decks)

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