Biological Molecules (Miss Reynolds)

Question 1

What atoms do organic compounds contain?

Answer 1

Carbon, hydrogen and oxygen.

Question 2

Polymer

Answer 2

A long molecule made of similar/identical units called monomers.

Question 3

Polysaccharides

Answer 3

Chain of carbohydrates, built from monosaccharides.

Question 4

Polymer for monosaccharides and example.

Answer 4

Carbohydrate (like starch)

Question 5

Polymer for amino acids and example.

Answer 5

Protein (e.g Insulin/collagen)

Question 6

Polymer for fatty acids and example.

Answer 6

Lipids (e.g fats/oils)

Question 7

Polymer for nucleotides.

Answer 7

DNA

Question 8

Name an example of a monosaccharide.

Answer 8

Glucose, fructose, ribose.

Question 9

Name an example of a disaccharide.

Answer 9

Lactose, sucrose.

Question 10

Name an example of a polysaccharide.

Answer 10

Glycogen, cellulose, starch.

Question 11

What’s the difference between alpha and beta glucose structurally?

Answer 11

The position of the OH-. In alpha it is below the carbon and in beta it is above.

Question 12

Which disaccharide out of maltose, sucrose and lactose has a beta glucose bond?

Answer 12

Lactose.

Question 13

Formula of glucose.

Answer 13

C6H12O6.

Question 14

Which polysaccharide out of cellulose, starch and glycogen uses beta glucose bonding?

Answer 14

Cellulose.

Question 15

Which polysaccharide is branched?

Answer 15

Glycogen.

Question 16

Similarities between all three polysaccharides.

Answer 16

All have glycosidic bonds and are insoluble.

Question 17

Reduction

Answer 17

A chemical reaction involving the gain of electrons/hydrogen.

Question 18

How to test for reducing sugars?

Answer 18

At Benedicts solution and if a brick red precipitate forms, reducing sugar is present.

Question 19

How to test for non-reducing sugars?

Answer 19

If there is no colour on Benedicts Test, add hydrochloric acid, hydrolysing any disaccharides into monosaccharides. Then add sodium hydrogen-carbonate solution to neutralise acid and repeat test.

Question 20

What is the bond in triglycerides?

Answer 20

Esther bonds.

Question 21

How do triglycerides form?

Answer 21

Condensation reaction.

Question 22

Lipids

Answer 22

A diverse group of compounds that are insoluble in water but soluble in organic solvents.

Question 23

In phospholipids what is hydrophilic and hydrophobic?

Answer 23

The phosphate is hydrophilic and fatty acids hydrophobic.

Question 24

Hydrophilic

Answer 24

Attracts water.

Question 25

Hydrophobic

Answer 25

Repels water.

Question 26

Name two roles of lipids.

Answer 26

An energy source, heat insulation, protection.

Question 27

Describe the emulsion test for lipids.

Answer 27

Adding ethanol to food sample and shake vigorously. Then add water and a milky layer will form if lipids present.

Question 28

What is the function of triglycerides?

Answer 28

Energy storage.

Question 29

Function of phospholipids?

Answer 29

Control what goes in/out of the cell.

Question 30

Proteins

Answer 30

A diverse group of large/complex polymer molecules.

Question 31

What are proteins made up of?

Answer 31

Long chains of amino acids.

Question 32

Structural proteins role.

Answer 32

Main component of body tissues e.g muscle/skin.

Question 33

Catalytic proteins role.

Answer 33

Biochemical reactions e.g enzymes.

Question 34

Signalling proteins role.

Answer 34

Cause body changes e.g hormones.

Question 35

Immunological proteins role.

Answer 35

Fight disease e.g antibodies.

Question 36

What defines an amino acid?

Answer 36

The R Group.

Question 37

What does the R Group represent?

Answer 37

A side chain from the central alpha carbon atom.

Question 38

Polypeptides

Answer 38

Long chains of amino acids.

Question 39

How do proteins/polypeptides form?

Answer 39

In condensation reactions.

Question 40

Primary protein structure.

Answer 40

Simple long chains with no intermolecular bonds.

Question 41

Secondary protein structure.

Answer 41

Hydrogen bonds form causing the molecule chain to either fold/coil. Forms alpha helix.

Question 42

Tertiary protein structure.

Answer 42

Hydrophilic/phobic interactions, hydrogen bonds, ionic bond and disulphide bonds hold the molecules together.

Question 43

Quaternary Protein Structure.

Answer 43

Same as tertiary but with two separate polypeptide chains interlinked.

Question 44

What causes proteins to denature?

Answer 44

The breaking of bonds.

Question 45

What factors lead to protein denature?

Answer 45

Temperature, pH, concentration.

Question 46

What happens to fibrous proteins when they denature?

Answer 46

They lose their structural strength and become insoluble and inactive.

Question 47

Structure of globular proteins.

Answer 47

Polypeptide chains are folded into spherical shapes, with the hydrophilic side chains on the outside, making them soluble.

Question 48

Structure of fibrous proteins.

Answer 48

Formed of long chains, several polypeptide chains can be cross linked for additional strength. Insoluble and important for structure.

Question 49

Name an example of a globular protein and fibrous one.

Answer 49

Globular, enzymes, fibrous, collagen/keratin.

Question 50

Digestion

Answer 50

Large biological molecules are hydrolysed by enzymes into smaller molecules that can be absorbed across the cell membrane.

Question 51

Amylase

Answer 51

Made by salivary glands and pancreas.

Question 52

Maltose

Answer 52

Made by small intestines.

Question 53

Miscelles

Answer 53

Tiny droplets of monoglyceride and fatty acids that release monoglycerids close to the surface of the cell.

Question 54

Endopeptidase

Answer 54

Hydrolyses peptide bonds within a polypeptide.

Question 55

Exopetidace

Answer 55

Hydrolyse peptide bonds at the end of the polypeptide.

Question 56

Endopeptidase

Answer 56

Stomach, produces small chains of amino acids by hydrolysing peptide bonds between amino acids.

Question 57

Physical Digestion

Answer 57

Breaking large pieces of food into smaller pieces.

Question 58

Chemical Digestion

Answer 58

Breaking down large molecules e.g starch.

Question 59

Digestive enzymes for the food groups.

Answer 59

Protein, protease, lipids, lipase, starch, maltose/amylase.

Question 60

Products of Digestion for each food group.

Answer 60

Protein, amino acids, lipids, fatty acids, starch, glucose.

Question 61

Membrane Bound Dipeptidase

Answer 61

Enzymes attached to membranes, hydrolyse peptide bonds between dipeptides.

Question 62

Exopeptidase

Answer 62

Ileum, produces single and pairs of amino acids by hydrolysing peptide bonds on the terminal amino acids.

Question 63

Dipeptidases

Answer 63

Ileum, produces single amino acids. (Membrane bound)

Question 64

Lock and Key Theory

Answer 64

The specific action of an enzyme with a single substrate.

Question 65

Induced-fit Theory

Answer 65

Substrate plays a roll in determining the final shape of the enzyme and that the enzyme is partially flexible.

Question 66

Rate

Answer 66

Amount of something produced per unit of time.

Question 67

What factors affect rate of reaction?

Answer 67

Temperature and concentration.

Question 68

As you increase concentration, rate of reaction increases, why?

Answer 68

More active sites for substrate molecules to react to.

Question 69

Whats the limiting factor with concentration?

Answer 69

Substrate as eventually there will be a point where there is more substrate than enzyme and the reaction cannot proceed any faster.

Question 70

Enzymes Inhibitors

Answer 70

Substances that interfere with the functioning of the active site of an enzyme and so reduce it’s activity.

Question 71

Competitive Inhibitors

Answer 71

Bind to the active site of the enzyme.

Question 72

Non-competitive inhibitors.

Answer 72

Bind to the enzyme at a position other than the active site.