KH3 Flashcards

1
Q

What’s another name for proteins?

A

“polypeptides”

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2
Q

What’s the biological purpose of DNA and RNA?

A

To allow the synthesis of proteins which carry physical/chemical functions of cells

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3
Q

What’s the average protein length? Smallest? Biggest?

A

300-400 // 40 // 30 000 (“Titin”)

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4
Q

What’s the primary structure of proteins?

A

The order/sequence of their amino acids

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5
Q

True or False? “Most proteins are rod-like or snake-like in shape”

A

False. They have their own unique 3D shape given by their primary structure.

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6
Q

Define hydrophilic

A

“Water loving”. Polar or charged groups that interact well with water (polar solvent)

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7
Q

Define hydrophobic

A

“Water fearing”. Non-polar groups that don’t interact well with water (polar solvent).

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8
Q

True or False? “It’s energetically favorable to keep non-polar particles apart in a polar medium”

A

False. Coalescence/Aggregation is better since more substance gets trapped within less total particles (leaves extra to flow freely). Also favored by Van der Waals.

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9
Q

From a general point of view, how do all proteins fold?

A

According to the oil drop model: hydrophilic outside and hydrophobic inside. (“Hydrophilic Shell”)

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10
Q

What does the Oil Drop model not account for?

A

Endless ways of achieving a Hydrophilic Shell but proteins only really adopt one or few structures in reality (“conformations”).

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11
Q

True or False? “Secondary and tertiary structures determine the path of the backbone through space”

A

True

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12
Q

Briefly differentiate secondary and tertiary structures

A

Secondary : local folding // Tertiary : final shape

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13
Q

What are domains in protein structure?

A

Regions of the chain that you could cut and they’d keep their shape (due to strong interactions within that area). Compact, usually longer than 40 monomers.

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14
Q

Define quaternary protein structure?

A

3D shape of multiple proteins interacting together.

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15
Q

True or False? “DNA directly dictates the protein function”

A

False. It’s indirect: DNA –> monomer order –> 3D shape –> function

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16
Q

What’s the directionality of a protein?

A

N terminus to C terminus

17
Q

What are the two major secondary conformations?

A

Alpha-helices and beta-sheets (account for 60% of chain length)

18
Q

What holds secondary structures together?

A

Hydrogen bonds between carbonyl O and amino H.

19
Q

True or False? “Surface properties of proteins only depend on side chains”

A

True. They stick out.

20
Q

What’s the effect of side chains on protein structure?

A

They influence conformation strength and how likely they are to form (affect interactions strength).

21
Q

True or False? “Beta-sheets link adjacent, antiparallel or parallel strands through H-bonds?”

A

True, which creates large flat surfaces.

22
Q

What are interactions that contribute to tertiary structure but not secondary?

A

Ionic bonds, Van der Waals, covalent bonds (S-S, “disulfide bridge)

23
Q

True or False? “Disulfide bonds could be both intrachain and interchain (quaternary structure)”

A

True

24
Q

What are motifs in protein structure?

A

Distinct and local 3D structures: heptad repeat, Ca binding, Zinc finger. Not structurally independent (too small).

25
Q

What are the four major structural protein classes?

A

“Fibrous” (linear), “Globular”, “Integral membrane” and “Intrinsically disordered” (exist as random coils until binds to partner protein).

26
Q

What are supramolecular complexes?

A

Large “molecular machines” made of many distinct proteins.

27
Q

True or False? “Protein structure, especially tertiary, can reveal ancient evolutionary relationships”

A

True

28
Q
A