Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biology Module 2 > 3.6, 3.7, Proteins, Types of Protein > Flashcards

3.6, 3.7, Proteins, Types of Protein Flashcards

(85 cards)

Start Studying
1
Q

What are the properties of each amino acid determined by?

A

Their Variable group

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

Describe the basic structure of an amino acid.

A

-There are 3 groups in an amino acid.
-One Amine group (NH2)
-One Carboxyl group (COOH)
-One Variable Group (R)

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

Are amino acids soluble or insoluble?

A

Amino acids are soluble in water, and form polar ions when added to water, some R groups are non-polar.

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

What are peptides?

A

Short chains made up of amino acid molecules

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

What determines what role the protein will play in the body?

A

The tertiary and quarternary structure of the protein.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are proteins made up of?

A

Polypeptides

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

What elements do all proteins contain?

A

Carbon, Hydrogen, Oxygen and Nitrogen

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

What group determines which amino acid it will be?

A

The R group.

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

How many different amino acids are there?

A

20

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

How is a dipeptide produced?

A

When the amine group of one amino acid and the carboxyl group of another react with eachother in a condensation reaction

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

What type of bond connects two amino acids together?

A

A peptide bond

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

What catalyses the reaction between two amino acids?

A

Peptidyl transferase

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

What type of reaction is it when polypeptide is broken down?

A

Hydrolysis reaction.

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

What determines the shape of a protein?

A

The sequence of the amino acids

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

What does the shape of a protein determine?

A

Its function

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

How many levels of protein structure are there? And what are their names?

A

4, Primary, Secondary, Tertiary, Quarternary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is the Primary Structure of a protein?

A

The sequence in which the amino acids are joined.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What are amino acids joined by in a polypeptide chain?

A

Peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What directs the sequence of amino acids?

A

Information carried within DNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What does the particular amino acids in a sequence influence?

A

How the polypeptide folds to give the protein’s final shape.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What is the Secondary Structure of proteins the result of?

A

Hydrogen bonds pulling polypeptide chains into different shapes.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

How is the Secondary Structure formed?

A

-The oxygen, nitrogen and hydrogen atoms of the repeating structure of the amino acids interact.
-Hydrogen bonds form within the amino acid chain and pull the structures into one of two shapes.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What are the two shapes found in secondary structure?

A

Alpha Helix or Beta Pleated Sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Do all proteins have a secondary structure?

A

Yes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
True or false: Proteins can only have one shape in their structure
False, proteins can have both alpha helixes AND beta pleated sheets in their structure, but the helix is the most common of the two
26
How do proteins form the secondary structure of an alpha helix?
Hydrogen bonds form WITHIN an amino acid chain, pulling it into a coiled shape, which is the alpha helix.
27
How do proteins form the secondary structure of a beta pleated sheet?
-Hydrogen bonds join SEPARATE polypeptide chains that lie parallel to eachother. -The pattern formed by the individual amino acids causes the structure to appear pleated (forming the shape of a beta-pleated sheet)
28
What is Tertiary Structure?
The folding of a protein into its final shape, that often involves sections of secondary structure.
29
What are the different types of interactions between R-Groups in Tertiary Structure?
-Hydrophobic and Hydrophilic interactions -Hydrogen bonds -Ionic bonds -Disulfide bonds/bridges
30
What are hydrophilic and hydrophobic interactions in Tertiary Structure?
Weak interactions between polar and non-polar R groups
31
What are hydrogen bonds in Tertiary Structure?
The weakest of the bonds formed
32
What are ionic bonds in Tertiary Structure? (how are they formed, what are they vulnerable to?)
Formed between oppositely charged R groups. Vulnerable to changes in pH
33
What are disulfide bonds in Tertiary Structure? (Type of bond, how are they formed?)
Covalent, and the strongest of the bonds. Only formed between R-groups that contain sulfur atoms, between adjacent cysteine molecules.
34
What is Quarternary Structure?
A result of the association of two or more individual polypeptide chains.
35
What makes Quarternary Structure similar to Tertiary Structure?
The interactions between the subunits are the same.
36
What types of subunits do Enzymes contain?
Two identical proteins
37
What types of subunits does Insulin contain?
Two different proteins
38
What polypeptide chains does haemoglobin contain?
Two alpha subunits, two beta subunits. ALSO a non-protein group known as a PROSTHETIC GROUP
39
What types of subunits does Haemoglobin contain?
4 subunits, made up of 2 sets of 2 identical proteins
40
What is haemoglobin required for?
Oxygen transport in the blood
41
Describe the group in Haemoglobin
It is a non-protein group known as a PROSTHETIC GROUP, called HEME, that contains Iron 2+. In one molecule of Haemoglobin, there are 4 FE2+ ions present.
42
What 3 groups can proteins be classified into?
Globular, conjugated and fibrous
43
What is the general shape of globular proteins?
Compact, spherical shape
44
What is the name for a protein without a prosthetic group?
Simple protein
45
Are globular proteins water soluble?
Yes
46
Why are globular proteins water soluble?
Because the Amino acids with hydrophobic R groups are on the inside of the sphere, and amino acids with hydrophilic R groups are on the outside. This is a feature of tertiary structure.
47
Are globular proteins affected by temp change and pH?
Yes, they denature at high temperatures and extreme pH.
48
Are globular proteins generally reactive or unreactive?
Reactive
49
Are globular proteins repetitive or not?
Not, there are few repetitive amino acid sequences
50
Give an example of a globular protein.
Insulin
51
What is insulin?
A globular, conjugated protein involved in the regulation of blood glucose concentration. It is soluble and precisely shaped
52
Why are globular proteins precisely shaped?
So that they can bond to complementary receptors on the plasma membrane of cells
53
State the features and properties of globular proteins.
-Precise 3D shape -Spherical -Soluble -Simple protein -Compact -Reactive -Affected by changes in pH and temp.
54
What is produced when a protein and a carbohydrate react?
A glycoprotein
55
What is produced when a protein and a lipid react?
A lipoprotein
56
What are conjugated proteins?
Globular proteins that contain a non-protein component (or prosthetic group)
57
What is a prosthetic group?
A non-protein component
58
List some of the different types of prosthetic groups.
Lipids, carbohydrates, metal ions, molecules derived from vitamins
59
What is the name of the prosthetic group that both Catalase and Haemoglobin contain?
Haem group
60
What is haemoglobin?
A red, oxygen-carrying pigment found in red blood cells. Contains a haem group, containing Fe2+ ions that can combine reversibly with an oxygen molecule, which enables it to transport oxygen around the bloodstream.
61
What enables haemoglobin to carry oxygen around the bloodstream?
The haem group which contains Fe2+ ions that can combine reversibly with an oxygen molecule
62
What is Catalase?
An enzyme that catalyses the breakdown of hydrogen peroxide.
63
What is hydrogen peroxide?
A common byproduct of the metabolism, damaging to cells and cell components if allowed to accumulate.
64
What are fibrous proteins?
Proteins formed from long, insoluble molecules that are strong.
65
Are fibrous proteins soluble?
No.
66
What makes fibrous proteins insoluble?
Contains a high proportion of amino acids with hydrophobic R groups, making them non-polar and therefore insoluble in water.
67
Do fibrous proteins have a repetitive structure? Why?
Yes, because there is a limited range of amino acids, usually with small R groups.
68
Why do fibrous proteins have very organised structures?
Because there are a limited range of amino acids, usually with small R groups
69
What are the general properties of Fibrous proteins?
Insoluble in water, flexible, unreactive, high tensile strength, not affected by changes in pH or temp.
70
Are there crosslinkages in fibrous proteins? Between what?
Yes, between amino acids of adjacent polypeptide chains.
71
List the structures that fibrous proteins have.
Repetitive primary structure, limited secondary structure (because they are not folded into 3D shapes), very limited tertiary structure.
72
Give some examples of fibrous proteins.
Keratin, Elastin, Collagen
73
Where is Keratin present?
In hair, skin and nails
74
What is a large proportion of keratin made of?
The amino acid Cysteine
75
What determines the flexibility of keratin?
The amount of disulfide bonds in the protein strand
76
What type of protein is Keratin?
Fibrous protein
77
What type of protein is Elastin?
Fibrous protein
78
What type of protein is Collagen?
Fibrous protein
79
What is collagen?
A fibrous protein and connective tissue
80
Where is collagen found?
Skin, tendons, ligaments.
81
What is a key property of collagen?
Flexible
82
Where is elastin found?
Walls of blood vessels, skin, and the alveoli in the lungs
83
What is the role of elastin?
To give the structures it is found in the flexibility to expand when needed
84
What is the quarternary structure of elastin made from?
Many stretchy molecules called tropoelastin
85
Describe a typical fibrous protein structure
-3 long parallel polypeptide chains -Hydrogen bonds forming cross-linkages between the chains, forming a tight triple helix.

Biology Module 2 (25 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions