Protein Structure Flashcards

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1
Q

What is the monomer of a protein

A

Amino acid

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2
Q

When does a dipeptide form?

A

When two amino acids join together

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3
Q

When does a polypeptide form?

A

When more than two amino acids join together

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4
Q

What are proteins made up of?

A

One or more popypeptides

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5
Q

Draw the structure of an amino acid

A

A carboxyl group joined to an amine group and an R group

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6
Q

How are polypeptides formed + describe?

A

Condensation reaction

A molecule of water is released during the reaction

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7
Q

Draw two amino acids undergoing a condensation reaction

A

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8
Q

Describe the primary structure of a protein

A

The sequence of amino acids in a polypeptide chain - joined by peptide bonds

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9
Q

Describe the secondary structure of a protein

A

Folding of the primary structure into an alpha helix or beta pleated sheet held together by hydrogen bonds

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10
Q

Describe the tertiary structure of a protein

A
Folding into a 3D structure using:
Hydrogen bonds 
Disulfide bridges
Ionic bonds
Hydrophobic and hydrophilic interactions
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11
Q

Describe the quaternary structure of a protein

A

Several popypeptides held together by bonds

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12
Q

Describe ionic bonds

A

Attractions between negative and positive charges on different parts of the molecule

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13
Q

Describe disulfide bridges

A

When two molecules of cysteine (amino acid) come close together, the sulfur atim in one systeine bonds to the sulfur in the other cysteine

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14
Q

Describe hydrophobic and hydrophilic interactions

A

When hydrophobic groups are close they clump together so that hydrophilic groups are pushed to the outside - affects the final folding of the protein

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15
Q

How does a proteins primary structure determine its 3D structure

A

Amino acid sequence determines what bonds will form and how the protein will fold which affects its properties

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16
Q

What are globular proteins?

A

Round, compact proteins made up of multiple polypeptide chains

17
Q

What are the polypeptide chains like in globular proteins? + what does this mean?

A

They are coiled so that the hydrophobic parts face inwards and the hydrophilic parts face outwards allowing the protein to be soluble

18
Q

Give an example of a globular protein

A

Hameoglobin:
Made of 4 polypeptide chains
Iron-containing haem groups that carry oxygen in the blood

19
Q

What are fibrous proteins?

A

Long insoluble polypeptide chains that are tightly coiled to form a rope shale

20
Q

What are the polypeptide chains like in fibrous proteins?

A

Held together by lots of bonds eg. Hydrogen and disulfide making the protein strong

21
Q

Where are fibrous proteins found?

A

In supportive tissue

22
Q

Give an example of a fibrous protein

A

Collagen is a strong, fibrous protein that forms connective tissuw

23
Q

What do enzymes do?

A

Catalyse metabolic reactions on a cellular level (respiration) and on a body lebel (digestion)

24
Q

What is a catalyst?

A

A substance that speeds up a chemical reaction without being used up in the reaction itself

25
Q

What makes enzymes highly specific?

A

Tertiary structure

26
Q

What is the active site?

A

The part of the enzyme where the substrate molecules bind to

27
Q

How do enzymes speed up the rate of reaction?

A

They lower activation energy making the reactions happen at a lower temperature

28
Q

How does an enzyme-substrate compelx lower the activation energy x2

A
  • if two substrates need joining, being attached to enzyme holds them closer together reducing repulsion between the molecules so can bond easier
  • if enzyme catalsyses a breakdown reaction, active sites put a strain on bonds so substrate molecules breaks easier
29
Q

Describe the lock and key model

A

The substrate fits into the enzyme the way a key fits into a lock

30
Q

Describe the induced fit theory

A

The active site changes shape as the substrate binds

31
Q

What determined the active sites shape?

A

The tertiary strucutr ehich is determined by the primary structure

32
Q

What is the primary sturcture determined by?

A

A gene - if a mutation occurs then the tertiary structure could be altered