7.1 Study Guide Flashcards

(11 cards)

1
Q

Protein structures are made up of what? and how much.

A

Monomers; 20 different monomers

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2
Q

Polypeptides are made up of polymers. Can proteins be made up of only 1 or more polypeptides?

A

Proteins can in fact be made up of 1 or more polypeptides.

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3
Q

What happens when a protein is put in conditions that disrupt and change the H bonds and ionic bonds?

A

Proteins denaturation happens, unfolding the protein.

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4
Q

What specifically causes denaturation in a protein?

A

Temperature, pH, and salinity

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5
Q

Can proteins, after denaturation, return to their functional shape?

A

Yes, through many cannot.

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6
Q

List the four protein structures:

A

Primary, secondary, tertiary, quaternary

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7
Q

How do hydrophobic side chains interact in a tertiary structure?

A

Hydrophobic side chains curve inwards in a tertiary structure.

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8
Q

How do hydrophilic side chains interact in a tertiary structure?

A

Hydrophilic side chains curve outwards in a tertiary structure.

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9
Q

How do Acidic and Basic side chains interact in a tertiary structure?

A

Acidic and Basic side chains curve towards each other due to opposite forces attracting each other.

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10
Q

How do Cysteine side chains interact in a tertiary structure?

A

Cysteine side chains curve inwards of the protein on the opposite side of each other. This is so they can form a covalent-disulfide bond, stabilizing the protein.

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11
Q

What happens when a hydrophobic amino acid is substituted for a hydrophilic?

A

A hydrophobic amino acid will curve inwards due to being water hating, hydrophilic side chains will curve outwards due to being water loving. Swapping a hydrophilic side chain with a hydrophobic side change will change the protein structure due it’s different properties, instead of curving outwards it will curve inwards, affecting all other side chains and causing shifts in side chain position in the protein structure.

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