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Biology 20 IB > Macromolecules > Flashcards

Macromolecules Flashcards

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1
Q

What are the primary functions (5) of carbohydrates?

A

Provide energy, short-term energy storage, plant cell wall structure (cellulose), backbone of DNA (ribose)

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2
Q

What are the 3 main monosaccharides?

A

Glucose, fructose, galactose

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3
Q

Which monosaccharides is maltose made up of?

A

2 Glucose

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4
Q

What monosaccharides are lactose made up of?

A

Galactose and Glucose

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4
Q

What monosaccharides is sucrose made up of?

A

Glucose and Fructose

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5
Q

How do you number carbons on glucose?

A

Start on the right, go counterclockwise

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5
Q

How do polymers form from monomers?

A

Dehydration synthesis

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5
Q

What is a polysaccharide?

A

Network of linked monosaccharides

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6
Q

What is the difference in the molecular structure of starch and cellulose?

A

Starch consists of alpha 1-4 glycosidic bonds (OH groups point in the same direction after synthesis) while cellulose consists of beta 1-4 glycosidic bonds (OH groups point in opposite directions).

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7
Q

Amylose bonding pattern

A

1-4 bonds with no branches

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8
Q

Amylopectin branching pattern

A

1-4 and 1-6 bonds with branches every 20 subunits

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9
Q

Glycogen bonding pattern

A

1-4 and 1-6 bonds with branches every 10 subunits

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10
Q

What are the three main polysaccharides?

A

cellulose, starch, and glycogen

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11
Q

How do polymers break apart into monomers?

A

Hydrolysis/catabolism

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12
Q

What is the role of glycogen?

A

Short term energy storage, it is broken down into usable monosaccharides when blood sugar is low

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13
Q

Another name for fats and oils

A

triglycerides

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14
Q

Which monomers is a triglyceride made up of?

A

One glycerol and Three fatty acids

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15
Q

How is cholestrol ingested?

A

Animal products

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16
Q

What are the main functions of lipids (4)?

A

Energy storage, insulation, cell membrane structure (phospholipids), precursors to steroid hormones (cholestrol)

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17
Q

What type of bonds are formed through dehydration synthesis of a triglyceride?

A

ester bonds

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18
Q

Is cholestrol a triglyceride?

A

No

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19
Q

Where is cholestrol produced?

A

Liver

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20
Q

What are the functions of cholestrol?

A

Stabilizes cell membrane, precursor for steroid hormones, help with brain and nerve cell function

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21
Q

How are saturated fatty acids ingested?

A

Animal products

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22
Q

How are unsaturated fatty acids ingested?

A

Plants

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23
Q

State of saturated vs unsaturated fatty acid at room temperature

A

Saturated is solid, unsaturated is liquid

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24
Q

What is the difference between saturated and unsaturated fatty acids?

A

Saturated fatty acids contain max H atoms, no double bonds. Unsaturated fatty acids have double bonds.

25
Q

Types of unsaturated fatty acids

A

Cis and Trans

26
Q

What’s the difference between cis and trans fatty acids

A

Cis- H atoms of double bonds are on the same side while on Trans, H atoms are on opposite side

27
Q

What makes trans fatty acids so hard to digest

A

H atoms being on opposite sides of double bond

28
Q

What’s another word for unsaturated fatty acid

A

oil

29
Q

What is the difference between an oil and a fat

A

Oil is liquid at RT (mainly unsaturated) while fat is solid at RT (mainly saturated)

30
Q

What percentage of dry mass do proteins make up in cells?

A

50%

31
Q

What is the monomer of a protein?

A

Amino acid

32
Q

How many total amino acids are there?

A

20

33
Q

How many amino acids are essential?

A

9, 11 can be synthesized

34
Q

What is the bond between amino acids called?

A

peptide bond

35
Q

Protein definition

A

polypeptide strand coiled into a 3D structure

36
Q

Primary structure of protein

A

Sequence of amino acids linked together by peptide bonds

37
Q

Secondary structure of protein

A

Hydrogen bonds form within amino acids, creating a helix shape

38
Q

Tertiary structure of protein

A

Hydrogen bonds and water molecules fold helix, disulfide bridges form between cysteine amino acids

39
Q

Quaternary structure of protein

A

Polypeptides are linked together by hydrogen bonds and disulfide bridges

40
Q

Enzymatic protein function

A

Accelerates certain chemical reactions

41
Q

Storage proteins

A

Store amino acids (Ex. casein stores amino acids in milk)

42
Q

Hormonal proteins

A

coordinates an organism’s activities (Ex. Insulin forces tissues to absorb glucose)

43
Q

Contractile and motor proteins

A

Responsible for movement (Actin and myosin)

44
Q

Defensive proteins

A

Protection against disease (Antibodies)

45
Q

Transport proteins

A

Transport, (Ex. hemoglobin transports oxygen from lungs to other parts of the body)

46
Q

Receptor proteins

A

Responsible for how the cell responds to chemical stimuli

47
Q

Structural proteins

A

Provide support (Collagen and elastin provide fibrous frameworks)

48
Q

What is an enzyme

A

A protein catalyst

49
Q

Definition of catalyst

A

Something that speeds up a reaction without being used up

50
Q

What is a substrate

A

Something that changes shape after binding to the active site of an enzyme

51
Q

Cofactors and coenzymes

A

Molecules that help with catalyzing chemical reactions

52
Q

What is the difference between a cofactor and a coenzyme

A

Cofactors are inorganic ions while coenzymes are organic molecules

53
Q

Lock and Key enzyme model

A

The active site has a rigid and specific shape, substrate must be enzyme-substrate specific

54
Q

How do substrates bind to the enzyme active site

A

Amino acid R groups may help, which forms the enzyme-substrate complex

54
Q

Induced fit model

A

Active site changes slightly so substrate fits

55
Q

What is the suffix of most enzymes

A

ase

56
Q

suffix of digestive enzymes

A

in

57
Q

Factors that can affect enzyme performance

A

Temperature, pH, substrate and enzyme concentration

58
Q

Denaturation

A

temperory alteration of enzyme shape

59
Q

Coagulation

A

Permanent alternation of enzyme shape

60
Q

Allosteric site

A

The part of an enzyme where substances can bind to that is not the active site

61
Q

What is an inhibitor

A

A molecule that slows down or stops chemical reaction

62
Q

Competitive vs non competitive inhibitor

A

Competitive inhibitor mimicks the substrate shape and directly competes with the substrate for the active site, while non competitive inhibitors bind to allosteric site (reduces function of enzyme)

63
Q

Feedback inhibition

A

Final product of reaction binds to first enzyme’s allosteric site, stopping production

Biology 20 IB (6 decks)

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