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Biology A Level > Proteins and Enzymes > Flashcards

Proteins and Enzymes Flashcards

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1
Q

What is the monomer in a protein?

A

An amino acid

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2
Q

What is the varying unit in an amino acid known as?

A

The R Group

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3
Q

What is the bond between two amino acids known as?

A

A peptide bond

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4
Q

What is the primary structure of a protein?

A

The order of amino acids

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5
Q

What is the secondary structure of a protein?

A

How the primary structure folds, into alpha helices or beta-pleated sheets

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6
Q

What is the tertiary structure of a protein?

A

How the alpha helices and beta-pleated sheets fold

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7
Q

What is the quaternary structure of a protein?

A

The structure of how multiple tertiary structures come together, involving prosthetic groups.

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8
Q

What forces are responsible for secondary structure of proteins?

A

Hydrogen bonds

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9
Q

What forces are responsible for the tertiary and quaternary structure of proteins ?

A

Hydrogen bonds
Ionic bonds
Disulphide bonds
Van de waal’s forces

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10
Q

What functional groups are attached to an amino acid?

A

Carboxylic acid group, amine group, and an R variable group

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11
Q

How many amino acids are there in the human body?

A

20

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12
Q

How do two amino acids bond together in terms of molecules?

A

The hydroxyl group on one amino acid and a hydrogen on another bond to form water and a dipeptide bond

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13
Q

What can break ionic bonds in proteins?

A

Changes to the pH

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14
Q

What can affect the rate that enzymes catalyse reactions ?

A 
Temperature
pH 
Concentration of enzymes
Concentration of substrates 
Pressure
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15
Q

What are intracellular enzymes?

A

Enzymes that function within the cell they are produced in (eg respiratory enzymes)

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16
Q

What are extracellular enzymes?

A

Enzymes that are secreted from the cell in which they are made and used elsewhere (eg amylase in saliva)

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17
Q

What do enzymes do?

A

They are organic catalysts, which mean they can speed up certain reactions by lowering the activation energy, without changing after the reaction

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18
Q

What are the two types of reactions that enzymes speed up?

A

Anabolic and catabolic reactions

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19
Q

What is an anabolic reaction (enzymes)?

A

A+B->AB

Ie building molecules, which often requires energy, meaning that they are endergonic

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20
Q

What is a catabolic reaction (enzymes)?

A

AB->A+B

Ie breaking down molecules, which often releases energy, meaning that they are exergonic

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21
Q

What do enzymes and their substrate combine to form?

A

An activated enzyme-substrate complex

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22
Q

Where do the substrate and enzyme come into contact at?

A

The active site

23
Q

What are the three types of cofactors that “help” enzymes?

A

Inorganic ions
Prosthetic groups
Coenzymes

24
Q

What do enzymes inhibitors do?

A

They reduce the rate of an enzymes reaction

25
Q

What are the two types of inhibitors?

A

Competitive and non-competitive enzyme inhibitors

26
Q

How do competitive inhibitors slow down enzymes?

A

They have a similar shape to the substrate, meaning they can fit into the active site and occupy it, preventing further formations of enzyme-substrate complex temporarily, slowing the rate of reaction.

27
Q

Describe the graph showing the effect of a competitive inhibitor to the rate of an enzymatic reaction

A

The line indicating “Without the inhibitor” has a steeper slope, before levelling off at a certain point, whereas the “with inhibitor” line has less steep slope, but levels off at the same point. This is because it slows the reaction, but doesn’t stop it.

28
Q

How do non-competitive inhibitors slow down enzymes?

A

Non-competitive inhibitors bind to the allosteric site which distorts the 3D tertiary structure, meaning that it prevents the formation of enzyme-product complexes, so it cannot catalyse a further reaction.

29
Q

Describe the graph showing the effect of a competitive inhibitor to the rate of an enzymatic reaction

A

The line indicating “Without the inhibitor” has a steeper slope, before levelling off at a certain point, whereas the “with inhibitor” line is less steep, and levels off at a lower point, as less enzymes can catalyse reactions.

30
Q

What enzymes break down carbohydrates?

A

Carbohydrases

31
Q

What enzymes break up proteins?

A

Proteases

32
Q

What enzymes break down lipids?

A

Lipases

33
Q

Describe the stages of digestion of carbohydrates

A

Starch is broken down into polysaccharides maltose in the lumen of the gut with amylase. This maltose is then broken down into monosaccharide glucose in the cells of the mucosa with maltase

34
Q

What are endopeptidases?

A

Enzymes found in the stomach that break down proteins, forming polypeptides. Ie breaking down bonds in the middle of the AA chain

35
Q

What are exopeptidases ?

A

Enzymes found in the stomach that break down polypeptides into dipeptides

36
Q

What are dipeptidases?

A

Enzymes found in the cells of gut mucosa or cell membrane of villi(intracellular) , that break down dipeptides into amino acids

37
Q

Describe the stages of protein digestion

A

Protein is catalysed using endopeptidase to form polypeptides, which is then catalysed using exopeptidase to form dipeptides, which is then catalysed using dipeptidase to form amino acids

38
Q

Where does lipid digestion occur?

A

In the lumen of the small intestine

39
Q

What is the process that breaks down lipids into smaller fat droplets?

A

A mechanical process called emulsification

40
Q

Describe the stages of lipid digestion

A

Lipids are broken down to form emulsified lipids (smaller lipid droplets) which are then catalysed into either fatty acids or glycerol using lipase

41
Q

Describe saliva

A

It is produced in the gastric glands, and works in the mouth. It contains amylase, which breaks down starch into maltose

42
Q

Describe gastric juice

A

It is produced in the gastric glands and works in the stomach. It contains endopeptidase, which breaks down proteins into polypeptides

43
Q

Describe pancreatic juice

A

It is produced in the pancreas, and works in the lumen of the small intestine. It contains amylase, endopeptidases, exopeptidases, and lipases

44
Q

Describe bile

A

It is produced in the liver, and works in the lumen of the small intestine. It doesn’t contain any enzymes, but emulsifiers lipids. It also increases the pH so that lipase can work. Contains bile salts and hydrogen carbonate

45
Q

Describe a villus (villi)

A

It has a thin epithelium (one cell thick to increase diffusion rate) with microvilli that increase surface area for absorption. It contains blood capillaries that absorb glucose and amino acids, and a lacteal (lymphatic vessel) that absorbs fatty acids and glycerol

46
Q

What is done to ensure that all glucose is absorbed into the cells?

A

Co transport with sodium, using the sodium-potassium pump

47
Q

Describe the co-transport of glucose and sodium

A

Glucose and sodium bind together, sodium moves down its concentration gradient into the cell (through facilitated diffusion).

48
Q

How is the low concentration of sodium maintained in the cell during the co-transport of glucose and sodium?

A

The sodium-potassium pump, where potassium is moved into the cell from the capillaries, and sodium is moved out of the cell into capillaries using active transport. This means less sodium is in the cell, maintaining the conc gradient

49
Q

What is formed to help the digestion of fats?

A

Micelles

50
Q

After fat digestion, describe how fats are transported to the cell

A

Monoglycerides and fatty acids associate with bile salts and phospholipids forming micelles. Micelles transport monoglycerides and fatty acids to the surface of the epithelial cell to be absorbed

51
Q

After fat digestion, describe what happens when fats are absorbed into the cell.

A

Once inside the epithelial cell, monoglycerides and fatty acids are resynthesised into triacylglycerol. These are then packaged with cholesterol and vitamins to form chylomicrons

52
Q

What are chylomicrons?

A

Chylomicrons are lipoproteins, which are special particles designed for the transport of lipids in circulation

53
Q

After fat digestion, describe what happens after the formation of chylomicrons

A

Vesicles carry chylomicrons to the opposite surface and are then released by exocytosis. They are too large to enter capillaries so enter lacteals, which then flow through circulation of the lymphatic system

Biology A Level (23 decks)

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