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Biology Exams > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the general structure of an amino acid?

A

A carbon with an amine group, a hydrogen, a carboxyl group and an R-group attached to it

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2
Q

What differs between different amino acids?

A

The only thing that changes from amino acids is the R-group

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3
Q

What type of bond is formed between amino acids?

A

A peptide bond

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4
Q

What is it called when two amino acids are joined?

A

A dipeptide

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5
Q

How do amino acids join?

A

Via condensation reactions

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6
Q

What is it called when many amino acids are joined?

A

Polypeptide

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7
Q

What enzymes catalyse the breakdown of peptides?

A

Proteases

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8
Q

How are peptides broken down into individual amino acids?

A

Via hydrolysis reactions (water is used to break the bond, reforming the amine and carboxyl groups)

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9
Q

What is primary protein structure?

A

The sequence in which amino acids are joined, as directed by DNA

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10
Q

What bonds are involved in primary structure?

A

Only peptide bonds

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11
Q

What is secondary protein structure?

A

The oxygen, hydrogen and nitrogen atoms of the basic structure of the amino acids interact

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12
Q

What new bonds are involved in secondary protein structure?

A

Hydrogen bonds form within the amino acid chain, forming one of two secondary structures

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13
Q

What are the two possible secondary protein structures?

A

Alpha helix or beta pleated sheet. It varies between the two depending on the amino acid composition

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14
Q

What is tertiary protein structure?

A

The folding of a protein into its final shape

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15
Q

How does secondary structure allow tertiary structure to develop?

A

The coiling or folding of sections of proteins in secondary structures bring R-groups of different amino acids close enough to interact

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16
Q

What new bonds are involved in tertiary protein structure?

A
  • Hydrophobic and hydrophillic interactions
  • Ionic bonds
  • Disulphide bridges
    (hydrogen bonds continue to form)
17
Q

What are hydrophobic and hydrophillic interactions?

A

Interactions between polar and non-polar R-groups

18
Q

What are ionic bonds?

A

Strong forces that form between oppositely charged R-groups

19
Q

What are disulphide bridges?

A

Strong covalent bonds that only form between R-groups that contain sulfur

20
Q

What is quaternary protein structure?

A

The association of two or more individual proteins (called subunits)

21
Q

What bonds are involved in quaternary protein structure?

A

Same as tertiary, except they are between different protein molecules (subunits) rather than within a single protein molecule

22
Q

What is the structure of globular proteins?

A

They fold in such a way that their hydrophobic R-groups are kept away from the aqueous environment, and their hydrophillic R-groups are on the outside

23
Q

What does the structure of globular proteins mean about its properties?

A

It means globular proteins are soluble

24
Q

Why is the solubility of globular proteins important (example)?

A

Insulin is a globular protein, and it has to be soluble as it is transported in the blood

25
Q

What are conjugated proteins?

A

Globular proteins that contain a non-protein component

26
Q

What is the non-protein component of conjugated proteins called?

A

The prosthetic group

27
Q

What is an example of enzyme which is a conjugated protein?

A

Catalase, which has a haem group (Fe2+) attached

28
Q

What is another example of a common conjugated protein?

A

Haemoglobin

29
Q

What is the structure of haemoglobin?

A

Haemoglobin is a quaternary protein, made from 4 subunits (2 beta, 2 alpha). Each subunit contains a prosthetic haem group (Fe2+)

30
Q

What are the properties of fibrous proteins?

A

Strong
Long
Insoluble
Not folded into complex 3d shapes (like globular proteins)

31
Q

What are 3 examples of fibrous proteins?

A

Keratin
Elastin
Collagen

32
Q

What are the properties and function of keratin?

A

Strong, inflexible and insoluble.

Found in hair, skin and nails

33
Q

What are the properties and function of elastin?

A

Adds flexibility and elasticity

Found in elastic fibres, which are present in the walls of blood vessels and aveoli

34
Q

What are the properties and function of collagen?

A

Flexible and strong

Found in connective tissue

35
Q

Why are fibrous protein not soluble in water?

A

They have a high proportion of hydrophobic R groups in their primary structures

Biology Exams (28 decks)

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