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Science for Medicine > Proteins > Flashcards

Proteins Flashcards

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1
Q

How many genetically amino acids are there?

A

20

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2
Q

What are the 4 basic categories of natural amino acids?

A

Acidic, basic, uncharged polar and non-polar

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3
Q

What are examples of acidic proteins?

A

Aspartic acid and glutamic acid (AG)

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4
Q

What are examples of basic proteins?

A

Lysine, arginine and histidine (LAH)

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5
Q

What are examples of uncharged polar proteins?

A

Asparagine, glutamine, serine, threonine and tyrosine (AGSTT)

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6
Q

What are examples of non-polar proteins?

A

Glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan and cysteine (GAVLIPPMTC)

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7
Q

How to proteins function?

A

By interacting with other biomolecules

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8
Q

What are the functions of protein?

A

Movement, protection, transport, enzymes, receptors, structural, storage, hormones and control of gene expression

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9
Q

What protein groups can be charged at biological pH?

A

Alpha-amino group, alpha-carboxyl group and R groups of some amino acid residues

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10
Q

What is the basic structure of proteins?

A

Unbranched linear polymer of L-amino acid residues linked by peptide bonds forming a polypeptide

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11
Q

What is the primary structure of proteins?

A

The sequence of amino acids in a polypeptide chain which is determined by gene encoding

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12
Q

What is the function of primary structured proteins?

A

They allow versatility in protein structure and function

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13
Q

What is the secondary structure of proteins?

A

The spatial arrangement of amino acid residues that are near each other in the linear sequence

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14
Q

What is an amino acid residue?

A

What remains of each amino acid after water is removed from the peptide

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15
Q

What are the 2 examples of secondary protein structures?

A

Alpha helices and beta sheets

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16
Q

What are alpha helices?

A

Telephone cord shape held in place by H bonds between the N-H group and the C=O group of each amino acid in the turn of the helix

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17
Q

What are beta sheets?

A

Pleated structure held together by H bonds between amide groups of linear polypeptide chains

18
Q

What is the tertiary structure of proteins?

A

The spatial arrangement of amino acid residues that are far apart in the linear chain

19
Q

What does the tertiary structure depend on?

A

Van der Waals, ionic interactions, H bonding, disulphide bridges and hydrophobic interactions

20
Q

What is the quaternary structure of proteins?

A

The spatial arrangement of individual polypeptide chains in a multi-subunit protein

21
Q

What are the properties of the quaternary structure?

A

Contains more than one polypeptide, can be fibrous or globular

22
Q

What causes a loss in 3D structure?

A

Denaturation

23
Q

What is denaturation?

A

Loss of 3D structure due to acid, heat or solvents. The primary structure is unaffected, while the secondary and tertiary structures are

24
Q

What does denaturation cause?

A

A decrease in solubility and a loss of function

25
Q

What is renaturation?

A

The gain of 3D structure

26
Q

What is the structure of fibrous proteins?

A

Beta-pleared sheet due to the interaction of many individual protein chains

27
Q

What determines the function of fibrous proteins?

A

It’s structure

28
Q

Where do fibrous proteins occur?

A

Bone matrices, muscle fibres, tendons and connective tissue

29
Q

What are examples of fibrous proteins?

A

Collagen, eleastins, keratins and fibrinogen

30
Q

What is the structure of globular proteins?

A

Clumped into a ball

31
Q

What are the functions of globular proteins?

A

Enzymes, messengers (hormones), transporters, amino acid storage and structural function

32
Q

What is an example of globular proteins?

A

Haemoglobin

33
Q

What are the 3 different types of modified proteins?

A

Glycoproteins, lipoproteins and metalloproteins

34
Q

What are glycoproteins?

A

They are carbohydrates that have joined to proteins which are formed by post-trasnlational modification. They are important integral membrane proteins and play a role in cell-cell interactions

35
Q

What are lipoproteins?

A

They are lipids joined to proteins. They transport water-insoluble fats in the blood e.g. HDL and LDL

36
Q

What are metalloproteins?

A

They are metals joined to proteins. They are used for enzymes, storage, signalling and transport

37
Q

What are examples of protein disorders?

A

Sickle cell anaemia, FH and scurvy

38
Q

What cases sickle cell anaemia?

A

One amino acid change

39
Q

What causes FH?

A

Decrease in LDL receptors

40
Q

What causes scurvy?

A

Weakened collagen

41
Q

What is an alpha-keto-acid?

A

The C skeleton of an alpha-amino-acid

42
Q

What is the difference between an alpha-keto-acid and an alpha-amino acid?

A

Alpha-keto-acids have been deaminated, although they have the same structure. The H and amino groups have been removed and replaced by an O group. The carbonyl and R groups are still there

Science for Medicine (19 decks)

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