Proteins 2 Flashcards

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1
Q

Give some examples of modified types of proteins?

A

Glycoproteins

Lipoproteins

Metalloproteins

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2
Q

What are glycoproteins?

A

Compound composed of protein and carbohydrates

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3
Q

How to glycoproteins occur?

A

From a post-translational modificaiton where a sugar molecule binds via an amino acid in the protein

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4
Q

What are some of the roles of glycoproteins?

A

Protein stabalisation

Affect solubility

Protein orientation

Signalling

Cell recognition

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5
Q

What is the process of forming a glycoprotein called?

A

Glycosylation

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6
Q

Where does glycosylation occur?

A

The endoplasmic reticulum and the golgi apparatus

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7
Q

What are some examples of glycoproteins?

A

Immunoglobulins

Blood group determinants

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8
Q

What are lipoproteins?

A

Proteins and lipids bonded together

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9
Q

What is the function of lipid proteins?

A

Transport insoluble fat and cholesterol in the blood

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10
Q

What are examples of lipoproteins?

A

High density lipoproteins (HDL)

Low density lipoproteins (LDL)

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11
Q

What are metalloproteins?

A

Protein molecules with a bound metal ion

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12
Q

What are some examples of metalloproteins?

A

Enzymes

Storage

Signilling

Transport

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13
Q

What are the three structures of proteins?

A

Globular (varied function)

Fibrous (structural function)

Membranous (associated with cell or orangelle membrane)

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14
Q

What are some examples of globular proteins?

A

Enzymes

Messengers (hormones)

Transporters

Stack of amino acids

Structural function such as actin or tubulin

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15
Q

What are some examples of fibrous proteins?

A

Bone matrices

Muscle fibres

Tendons

Connective tissue

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16
Q

What are some examples of membranous proteins?

A

Relay signal

Membrane transporter

Membrane enzyme

Cell adhesion molecule

17
Q

What is a specific example of a globular protein?

A

Haemoglobin

18
Q

How does haemoglobin operate?

A

Carries O2

Haem group at the centre of each polypeptide chain binds to a moleucle of O2

Composed of 4 units, so you can carry 4 molecules of O2

19
Q

What does the binding of O2 do to the shape of haemoglobin?

A

Changes its conformaiton which allows for more O2 to bind easier

20
Q

What is cooperative binding?

A

When a molecules binds to a protein and makes it easier for other molecules to bind

21
Q

What is a specific example of a fibrous protein?

A

Collagen

22
Q

What is the structure of collagen?

A

Three polypeptide chains coil around each other

Held together by hydrogen bonds

Composed of repeated units (glycine - x - proline)n

where x = alanine, hydroxyproline or lysine)

23
Q

What happens when collagen interacts with each other?

A

They form fibriles and increase strength

24
Q

What kind of receptors are present in all cells and what do they allow?

A

LDL receptors

They allow the internalisation of LDL which is then broken down in lysosomes

25
Q

What are 5 possible classes of LDL receptor mutations?

A
  1. Class 1 - no receptor produced
  2. Class 2 - receptor never reach the cell surface
  3. Class 3 - receptor can’t bind to LDL
  4. Class 4 - receptors don’t internalise on binding
  5. Class 5 - receptors don’t release LDL