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Biology 🍃 > Biological Molecules (Miss Reynolds) > Flashcards

Biological Molecules (Miss Reynolds) Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What atoms do organic compounds contain?

A

Carbon, hydrogen and oxygen.

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2
Q

Polymer

A

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

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3
Q

Polysaccharides

A

Chain of carbohydrates, built from monosaccharides.

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4
Q

Polymer for monosaccharides and example.

A

Carbohydrate (like starch)

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5
Q

Polymer for amino acids and example.

A

Protein (e.g Insulin/collagen)

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6
Q

Polymer for fatty acids and example.

A

Lipids (e.g fats/oils)

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7
Q

Polymer for nucleotides.

A

DNA

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8
Q

Name an example of a monosaccharide.

A

Glucose, fructose, ribose.

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9
Q

Name an example of a disaccharide.

A

Lactose, sucrose.

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10
Q

Name an example of a polysaccharide.

A

Glycogen, cellulose, starch.

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11
Q

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

A

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

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12
Q

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

A

Lactose.

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13
Q

Formula of glucose.

A

C6H12O6.

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14
Q

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

A

Cellulose.

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15
Q

Which polysaccharide is branched?

A

Glycogen.

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16
Q

Similarities between all three polysaccharides.

A

All have glycosidic bonds and are insoluble.

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17
Q

Reduction

A

A chemical reaction involving the gain of electrons/hydrogen.

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18
Q

How to test for reducing sugars?

A

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

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19
Q

How to test for non-reducing sugars?

A

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.

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20
Q

What is the bond in triglycerides?

A

Esther bonds.

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21
Q

How do triglycerides form?

A

Condensation reaction.

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22
Q

Lipids

A

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

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23
Q

In phospholipids what is hydrophilic and hydrophobic?

A

The phosphate is hydrophilic and fatty acids hydrophobic.

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24
Q

Hydrophilic

A

Attracts water.

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25
Q

Hydrophobic

A

Repels water.

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26
Q

Name two roles of lipids.

A

An energy source, heat insulation, protection.

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27
Q

Describe the emulsion test for lipids.

A

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

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28
Q

What is the function of triglycerides?

A

Energy storage.

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29
Q

Function of phospholipids?

A

Control what goes in/out of the cell.

30
Q

Proteins

A

A diverse group of large/complex polymer molecules.

31
Q

What are proteins made up of?

A

Long chains of amino acids.

32
Q

Structural proteins role.

A

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

33
Q

Catalytic proteins role.

A

Biochemical reactions e.g enzymes.

34
Q

Signalling proteins role.

A

Cause body changes e.g hormones.

35
Q

Immunological proteins role.

A

Fight disease e.g antibodies.

36
Q

What defines an amino acid?

A

The R Group.

37
Q

What does the R Group represent?

A

A side chain from the central alpha carbon atom.

38
Q

Polypeptides

A

Long chains of amino acids.

39
Q

How do proteins/polypeptides form?

A

In condensation reactions.

40
Q

Primary protein structure.

A

Simple long chains with no intermolecular bonds.

41
Q

Secondary protein structure.

A

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

42
Q

Tertiary protein structure.

A

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

43
Q

Quaternary Protein Structure.

A

Same as tertiary but with two separate polypeptide chains interlinked.

44
Q

What causes proteins to denature?

A

The breaking of bonds.

45
Q

What factors lead to protein denature?

A

Temperature, pH, concentration.

46
Q

What happens to fibrous proteins when they denature?

A

They lose their structural strength and become insoluble and inactive.

47
Q

Structure of globular proteins.

A

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

48
Q

Structure of fibrous proteins.

A

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

49
Q

Name an example of a globular protein and fibrous one.

A

Globular, enzymes, fibrous, collagen/keratin.

50
Q

Digestion

A

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

51
Q

Amylase

A

Made by salivary glands and pancreas.

52
Q

Maltose

A

Made by small intestines.

53
Q

Miscelles

A

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

54
Q

Endopeptidase

A

Hydrolyses peptide bonds within a polypeptide.

55
Q

Exopetidace

A

Hydrolyse peptide bonds at the end of the polypeptide.

56
Q

Endopeptidase

A

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

57
Q

Physical Digestion

A

Breaking large pieces of food into smaller pieces.

58
Q

Chemical Digestion

A

Breaking down large molecules e.g starch.

59
Q

Digestive enzymes for the food groups.

A

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

60
Q

Products of Digestion for each food group.

A

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

61
Q

Membrane Bound Dipeptidase

A

Enzymes attached to membranes, hydrolyse peptide bonds between dipeptides.

62
Q

Exopeptidase

A

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

63
Q

Dipeptidases

A

Ileum, produces single amino acids. (Membrane bound)

64
Q

Lock and Key Theory

A

The specific action of an enzyme with a single substrate.

65
Q

Induced-fit Theory

A

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

66
Q

Rate

A

Amount of something produced per unit of time.

67
Q

What factors affect rate of reaction?

A

Temperature and concentration.

68
Q

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

A

More active sites for substrate molecules to react to.

69
Q

Whats the limiting factor with concentration?

A

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

70
Q

Enzymes Inhibitors

A

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

71
Q

Competitive Inhibitors

A

Bind to the active site of the enzyme.

72
Q

Non-competitive inhibitors.

A

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

Biology 🍃 (10 decks)

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