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Biology Module 2, Chapter 3 - Biological Molecules > Proteins (Structure) > Flashcards

Proteins (Structure) Flashcards

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1
Q

What are the monomeric units of proteins?

A

Amino acids

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2
Q

Where do we get amino acids from?

A

Our diet

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3
Q

What elements do all proteins contain?

A

Carbon
Hydrogen
Oxygen
Nitrogen
Sulfur

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4
Q

Outline the journey an amino acid takes from food to protein in a cell

HINT: FRED EATS APPLES TO POWER UP

A

F - Food is ingested.
E - Enzymes break down proteins in the stomach and small intestine.
A - Amino acids are absorbed into the blood.
T - Amino acids travel through tissue fluid to cells.
P - Proteins are synthesized on ribosomes.

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5
Q

How many common amino acids are there?

A

20

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6
Q

How many amino acids are classified as non-essential, and why?

A

5 - body can synthesise them from other amino acids.

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7
Q

How many amino acids are classified as essential, and why?

A

9 - Needed by infants and growing children for growth.

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8
Q

Give 4 functions of proteins

A

enzymes
hormones
antibodies
structural proteins

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9
Q

What do the interactions of differing R-groups determine?

A

The folding of the protein

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10
Q

What type of reaction occurs to form a protein from 2 amino acids?

A

Condensation

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11
Q

What type of bond is formed from the synthesis of a protein?

A

Peptide

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12
Q

What is produced in the condensation reaction between two amino acids?

A

Water and dipeptide

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13
Q

What is the general formula of an amino acid?

A

R-CH(NH2)-COOH

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14
Q

What determines the differences between amino acids?

A

The differences between amino acids are determined by their R groups, also known as variable groups.

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15
Q

Between which parts of the amino acid molecules does the condensation reaction between two amino acids occur?

A

The carboxyl group of one amino acid and the amine group of another amino acid

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16
Q

How are amino acids joined together?

A

Amino acids join when the amine group of one reacts with the carboxylic acid group of another, forming a peptide bond and releasing water.

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17
Q

What is a chain of amino acids called?

A

A polypeptide

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18
Q

What are peptides? How do they make up proteins?

A

Peptides are polymers that are made-up of amino acid molecules which are the monomers.

Proteins consist of one or more polypeptides that are arranged as complex macromolecules, and they have a specific biological function.

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19
Q

What is the end of a polypeptide with an amino group called?

A

The N-terminus

20
Q

What is the end of the polypeptide with a carboxyl group called?

A

The C-terminus

21
Q

What is produced when two amino acids join together?

A

A dipeptide and a molecule of water are produced.

22
Q

What is formed when many amino acids are joined by peptide bonds?

A

A polypeptide is formed.

23
Q

What enzyme catalyses the formation of peptide bonds, and when? Where is found?

A

Peptidyl transferase, an enzyme found in ribosomes, catalyses the formation of peptide bonds during protein synthesis.

24
Q

How do R groups influence protein structure?

A

The R groups interact with each other, forming various bonds that cause the polypeptide chain to fold into complex, specific structures.

25
Q

Why is the specific shape of a protein important?

A

The unique shape of a protein is crucial for its specific functions in living organisms.

26
Q

How does the sequence of amino acids affect a protein’s structure?

A

Different sequences of amino acids lead to different folding patterns and protein shapes, which are vital for diverse protein functions.

27
Q

What defines the primary structure of a protein?

A

The primary structure is the sequence of amino acids in a polypeptide chain, determined by the DNA sequence.

28
Q

What bonds are found in the primary structure of protein?

A

Peptide bonds are the only bonds involved in the primary structure.

29
Q

What shape is the primary structure of a protein?

A

Linear

30
Q

What forms the secondary structure of a protein?

A

The folding of the primary structure

31
Q

What bonds are involved in the secondary structure of proteins?

A

The secondary structure is held together by hydrogen bonds between the oxygen, hydrogen, and nitrogen atoms of the amino acids.

32
Q

What are the two common shapes formed in the secondary structure of proteins?

A

The two common shapes are the alpha helix (a coiled shape) and the beta-pleated sheet (a zigzag or folded shape).

33
Q

In the secondary structure, what do hydrogen bonds form between?

A

Partially positive H and partially negative O

34
Q

What defines the tertiary structure of a protein? What is it formed by? What is the folding influenced by?

A

The tertiary structure is the final 3D shape of a protein, formed by the folding of the polypeptide chain (secondary structure). This folding is influenced by interactions between R groups.

35
Q

What are the 4 types of bond formed at the tertiary level of structure?

A

Hydrophobic and hydrophilic interactions
Hydrogen bonds
Ionic bonds
Disulfide bonds

36
Q

What do hydrophobic and hydrophilic interactions form between?

A

Polar and non-polar R-groups

37
Q

What do hydrogen bonds form between?

A

Partially positive H and partially negative O (weak bonds between polar R groups)

38
Q

What do ionic bonds form between?

A

Positively and negatively charged ions (stronger bonds between oppositely charged R groups)

39
Q

What do disulfide bridges form between?

A

Sulphur atoms contained within R-groups

40
Q

Which amino acid contains sulphur?

A

Cysteine

41
Q

What defines the quaternary structure of a protein?

HINT: Queen Polly Interacts Gracefully

A

Q - Quaternary Structure: This is the highest level of protein structure, formed by multiple subunits.

P - Polypeptide Subunits: The structure forms when two or more polypeptide subunits interact.

I - Identical or Different: These subunits can be either identical or different.

G - Groups (Prosthetic): The structure can include prosthetic groups (non-protein components that assist in protein function).

42
Q

What type of bonds holds together the quaternary structure?

A

ionic
hydrogen
disulfide
hydrophobic and hydrophilic interactions

43
Q

What are examples of proteins with quaternary structure?

A

Examples include:
enzymes (which often consist of identical subunits)
insulin (which has two different subunits)
haemoglobin (which has four subunits, made up of two sets of two identical subunits).

44
Q

How does the hydrophilic or hydrophobic nature of R groups affect protein folding?

A

Hydrophilic R groups are on the outside of the protein, interacting with water, while hydrophobic R groups are shielded inside the protein, away from the water in the cytoplasm.

45
Q

What is a prosthetic group?

A

a non-protein component of a conjugated protein

46
Q

What are simple proteins?

A

Proteins without a prosthetic group

Biology Module 2, Chapter 3 - Biological Molecules (6 decks)

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