3.7 - Types of proteins (new) Flashcards

(45 cards)

1
Q

What is a globular protein?

A

Spherical Water-soluble proteins

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2
Q

Give 3 characteristics of globular proteins

A
  • compact
  • water soluble
  • roughly spherical
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3
Q

Why are globular proteins water soluble?

A

TERTIARY structures are folded so that the hydrophobic R-groups are kept away from the aqueous environment -hydrophilic R-groups are on the outside

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4
Q

What is an example of a globular protein and its function?

A

Insulin is a globular protein that regulates blood glucose levels. It is soluble in the bloodstream and has a precise shape to bind to specific receptors on cell membranes.

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4
Q

Why is the solubility of globular proteins important?

A

The solubility allows globular proteins to perform vital functions in the body, such as chemical reactions, immunity, and muscle contraction.

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5
Q

What is insulin made up of?

A

Insulin is made up of two polypeptide chains held together by disulphide bonds.

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6
Q

What are globular proteins used for?

A

Catalysing reactions, Regulating processes, and immune response.

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7
Q

Give examples of the processes globular proteins regulate

A
  • Muscle contraction
  • Immunity
  • Chemical processes
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8
Q

What metabolic roles do globular proteins have in the body?

A
  • Enzymes - These speed up chemical reactions in the body.
  • Hormones - These are chemical messengers that travel in the bloodstream.
  • Antibodies - These bind to and prevent the spread of pathogens.
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9
Q

Are conjugated proteins a type of globular protein?

A

Yes.

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10
Q

What is amylase? What is its role? What is it made up of?

A
  • Amylase is a globular protein known as an enzyme. It is responsible for the breakdown of starch into maltose.
  • This enzyme is made up of a single polypeptide chain folded using both alpha-helixes and beta-pleated sheets.
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11
Q

What are conjugated proteins?

A

Conjugated proteins are globular proteins that contain a non-protein component called a prosthetic group. Proteins without prosthetic groups are called simple proteins.

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12
Q

What do conjugated proteins contain?

A

A non-protein prosthetic group

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13
Q

What is a prosthetic group and give an example?

A

A prosthetic group is a non-protein component that binds to a protein, such as a metal ion or molecule derived from vitamins.

An example is the haem group, which contains an iron ion (Fe²⁺).

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14
Q

Give an example of 2 conjugated proteins

A
  • Haemoglobin
  • Catalase
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14
Q

What is the function of haemoglobin?

A

Carries oxygen in the blood in erythrocytes

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15
Q

What polypeptide subunits is haemoglobin made up of?

A

2 alpha-helices 2 beta-pleated sheets

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15
Q

How many subunits make up haemoglobin?

A

4

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16
Q

What does each haem group contain?

16
Q

What does each subunit of haemoglobin contain?

17
Q

How do haem groups allow erythrocytes to carry out their function?

A

Iron ions in haem groups can reversibly combine with an oxygen molecule

18
Q

How many oxygen atoms can one haemoglobin molecule carry?

A

8- remember ATOMS not MOLECULES

19
Q

How does haemoglobin transport oxygen?

A
  • Haemoglobin is a quaternary protein with four polypeptide subunits (two alpha and two beta) and prosthetic haem groups.
  • Each haem group can bind reversibly with an oxygen molecule, allowing haemoglobin to pick up oxygen in the lungs and release it in tissues.
19
Q

What type of protein is catalase?

19
What type of prosthetic group does catalase contain?
Haem
20
What is catalase and how does it function? What does it produce?
Catalase is a quaternary protein containing haem groups, which allows it to catalyse the breakdown of hydrogen peroxide, a harmful by-product of metabolism, into water and oxygen.
21
How many haem groups does catalase contain?
4
22
What is a fibrous protein?
Long, insoluble, structural proteins
23
What are the characteristics of fibrous proteins?
Fibrous proteins are long, insoluble molecules with a high proportion of hydrophobic R groups. They typically have a repetitive primary structure, which leads to organised, strong, and often unstructured forms.
24
Give 3 examples of fibrous proteins.
* Collagen * Elastin * Keratin
25
Where is Keratin found?
In hair, skin, and nails
26
Which amino acid does keratin contain in a high proportion?
Cysteine
27
What does Cysteine contain in its R-group?
Sulfur
28
What type of bonding occurs a lot in keratin?
Disulphide bonds
29
How does a high proportion of disulphide affect the properties of keratin?
It makes it inflexible and strong
29
Where is elastin found?
In the walls of blood vessels and alveoli of lungs
30
Why is it beneficial for tissues to contain elastin?
It confers strength and elasticity
30
What does elastin allow tissues to do?
Expand and return to size
31
What makes up elastin?
Aggregates of tropoelastin
32
Where is collagen found?
In the skin, tendons, ligaments, and nervous system
33
What is the structure of collagen?
Collagen is made up of three polypeptide chains wound around each other in a rope-like structure. This provides strength and flexibility to the molecule.
34
Why does collagen contain glycine for every 3rd amino acid?
Glycine is the smallest amino acid and so they can pack together more tightly
35
What property does collagen have?
Flexibility
36
Define polypeptide.
Chains of 3 or more amino acids
37
Define protein.
One or more polypeptides arranged as a complex macromolecule