Proteins Flashcards

1
Q

What elements do proteins contain?

A

Carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the sub-units from which proteins are formed?

A

Amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the generalized structure of an amino acid?

A

H2N, COOH, and a carbon-containing side group R.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

How many different commonly occurring amino acids are there in living organisms?

A

20.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What groups do all amino acids have?

A
  • Amine group (NH2)
  • Carboxylic acid group (COOH)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What type of bond joins amino acids together?

A

Peptide bonds (-CONH-).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What reaction forms a dipeptide?

A

Condensation reaction between two amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What do many amino acids joined together form?

A

A polypeptide.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What may a protein consist of?

A

One or more polypeptides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What process can hydrolyze proteins?

A

Heating with acid or using enzymes (proteases).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Fill in the blank: Amino acids are joined together by _______.

A

Peptide bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

True or False: Proteins can only be hydrolyzed by heating with acid.

A

False.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What determines the primary structure of proteins?

A

The sequence of amino acids in the polypeptide chain

The primary structure is crucial as it dictates the protein’s shape and function.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the two main types of secondary structures in proteins?

A

Alpha helix and beta-pleated sheet

These structures arise from hydrogen bonding between amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What type of bonds contribute to the tertiary structure of proteins?

A

Hydrogen bonds, ionic bonds, and disulfide bonds

The tertiary structure is influenced by the sequence of amino acids in the primary structure.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

How does the tertiary structure of an enzyme affect its function?

A

It determines the shape of its active site

The active site shape is critical for enzyme-substrate interactions.

17
Q

What characterizes globular proteins?

A

They are soluble and consist of a highly folded and coiled polypeptide chain

Examples include enzymes and antibodies.

18
Q

What is the quaternary structure of proteins?

A

When proteins consist of more than one polypeptide chain

These chains are held together by ionic bonds, hydrogen bonds, and sometimes disulfide bonds.

19
Q

Fill in the blank: The _______ structure refers to the sequence of amino acids in the polypeptide chain.

A

primary

The primary structure is foundational for protein formation.

20
Q

True or False: The secondary structure of proteins is solely determined by the primary structure.

A

True

The folding and coiling in secondary structure arise from interactions dictated by the primary structure.

21
Q

What is the significance of the R groups of amino acids in protein structure?

A

They determine the formation of tertiary structure through bonding

The unique interactions between R groups lead to the specific shape and function of proteins.

22
Q

List the types of bonds involved in stabilizing tertiary structure.

A
  • Hydrogen bonds
  • Ionic bonds
  • Disulfide bonds

These bonds contribute to the protein’s overall stability and functionality.

23
Q

What type of protein structure is characterized by more than one polypeptide chain?

A

Quaternary structure

This structure is important for the function of many multi-subunit proteins.

24
Q

What is denaturation of proteins?

A

An alteration in the tertiary structure of a protein, leading to a loss of its three-dimensional shape and functionality.

Denaturation is often irreversible.

25
Q

What usually causes denaturation of proteins?

A

Breaking of hydrogen and ionic bonds, high temperatures above the optimum, extreme changes in pH, and heavy metals.

Heavy metals can also contribute to denaturation.

26
Q

Are disulfide bonds broken during protein denaturation at typical temperatures?

A

No, disulfide bonds are not broken at the temperatures that break hydrogen and ionic bonds.

Some proteins can have disulfide bonds remain unbroken at 70 °C.

27
Q

What is the Biuret test used for?

A

To test a sample for the presence of protein.

A specific reagent is used in this test.

28
Q

What indicates the presence of protein in the Biuret test?

A

A purple or lilac color indicates protein is present.

If the solution remains blue, no protein is present.

29
Q

Fill in the blank: Denaturation is often _______.

A

irreversible

30
Q

What happens to the functionality of a protein after denaturation?

A

The protein is no longer functional.

This is a key consequence of denaturation.

31
Q

True or False: Denaturation can be caused by extreme changes in pH.

32
Q

List three factors that can lead to protein denaturation.

A
  • High temperatures above the optimum
  • Extreme changes in pH
  • Heavy metals