Proteins (Structure) Flashcards

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
Why is the specific shape of a protein important?
The unique shape of a protein is crucial for its specific functions in living organisms.
26
How does the sequence of amino acids affect a protein’s structure?
Different sequences of amino acids lead to different folding patterns and protein shapes, which are vital for diverse protein functions.
27
What defines the primary structure of a protein?
The primary structure is the sequence of amino acids in a polypeptide chain, determined by the DNA sequence.
28
What bonds are found in the primary structure of protein?
Peptide bonds are the only bonds involved in the primary structure.
29
What shape is the primary structure of a protein?
Linear
30
What forms the secondary structure of a protein?
The folding of the primary structure
31
What bonds are involved in the secondary structure of proteins?
The secondary structure is held together by hydrogen bonds between the oxygen, hydrogen, and nitrogen atoms of the amino acids.
32
What are the two common shapes formed in the secondary structure of proteins?
The two common shapes are the alpha helix (a coiled shape) and the beta-pleated sheet (a zigzag or folded shape).
33
In the secondary structure, what do hydrogen bonds form between?
Partially positive H and partially negative O
34
What defines the tertiary structure of a protein? What is it formed by? What is the folding influenced by?
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
What are the 4 types of bond formed at the tertiary level of structure?
Hydrophobic and hydrophilic interactions Hydrogen bonds Ionic bonds Disulfide bonds
36
What do hydrophobic and hydrophilic interactions form between?
Polar and non-polar R-groups
37
What do hydrogen bonds form between?
Partially positive H and partially negative O (weak bonds between polar R groups)
38
What do ionic bonds form between?
Positively and negatively charged ions (stronger bonds between oppositely charged R groups)
39
What do disulfide bridges form between?
Sulphur atoms contained within R-groups
40
Which amino acid contains sulphur?
Cysteine
41
What defines the quaternary structure of a protein? HINT: Queen Polly Interacts Gracefully
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
What type of bonds holds together the quaternary structure?
ionic hydrogen disulfide hydrophobic and hydrophilic interactions
43
What are examples of proteins with quaternary structure?
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
How does the hydrophilic or hydrophobic nature of R groups affect protein folding?
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
What is a prosthetic group?
a non-protein component of a conjugated protein
46
What are simple proteins?
Proteins without a prosthetic group