Macromolecules Flashcards

(67 cards)

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
How are unsaturated fatty acids ingested?
Plants
23
State of saturated vs unsaturated fatty acid at room temperature
Saturated is solid, unsaturated is liquid
24
What is the difference between saturated and unsaturated fatty acids?
Saturated fatty acids contain max H atoms, no double bonds. Unsaturated fatty acids have double bonds.
25
Types of unsaturated fatty acids
Cis and Trans
26
What's the difference between cis and trans fatty acids
Cis- H atoms of double bonds are on the same side while on Trans, H atoms are on opposite side
27
What makes trans fatty acids so hard to digest
H atoms being on opposite sides of double bond
28
What's another word for unsaturated fatty acid
oil
29
What is the difference between an oil and a fat
Oil is liquid at RT (mainly unsaturated) while fat is solid at RT (mainly saturated)
30
What percentage of dry mass do proteins make up in cells?
50%
31
What is the monomer of a protein?
Amino acid
32
How many total amino acids are there?
20
33
How many amino acids are essential?
9, 11 can be synthesized
34
What is the bond between amino acids called?
peptide bond
35
Protein definition
polypeptide strand coiled into a 3D structure
36
Primary structure of protein
Sequence of amino acids linked together by peptide bonds
37
Secondary structure of protein
Hydrogen bonds form within amino acids, creating a helix shape
38
Tertiary structure of protein
Hydrogen bonds and water molecules fold helix, disulfide bridges form between cysteine amino acids
39
Quaternary structure of protein
Polypeptides are linked together by hydrogen bonds and disulfide bridges
40
Enzymatic protein function
Accelerates certain chemical reactions
41
Storage proteins
Store amino acids (Ex. casein stores amino acids in milk)
42
Hormonal proteins
coordinates an organism's activities (Ex. Insulin forces tissues to absorb glucose)
43
Contractile and motor proteins
Responsible for movement (Actin and myosin)
44
Defensive proteins
Protection against disease (Antibodies)
45
Transport proteins
Transport, (Ex. hemoglobin transports oxygen from lungs to other parts of the body)
46
Receptor proteins
Responsible for how the cell responds to chemical stimuli
47
Structural proteins
Provide support (Collagen and elastin provide fibrous frameworks)
48
What is an enzyme
A protein catalyst
49
Definition of catalyst
Something that speeds up a reaction without being used up
50
What is a substrate
Something that changes shape after binding to the active site of an enzyme
51
Cofactors and coenzymes
Molecules that help with catalyzing chemical reactions
52
What is the difference between a cofactor and a coenzyme
Cofactors are inorganic ions while coenzymes are organic molecules
53
Lock and Key enzyme model
The active site has a rigid and specific shape, substrate must be enzyme-substrate specific
54
How do substrates bind to the enzyme active site
Amino acid R groups may help, which forms the enzyme-substrate complex
54
Induced fit model
Active site changes slightly so substrate fits
55
What is the suffix of most enzymes
ase
56
suffix of digestive enzymes
in
57
Factors that can affect enzyme performance
Temperature, pH, substrate and enzyme concentration
58
Denaturation
temperory alteration of enzyme shape
59
Coagulation
Permanent alternation of enzyme shape
60
Allosteric site
The part of an enzyme where substances can bind to that is not the active site
61
What is an inhibitor
A molecule that slows down or stops chemical reaction
62
Competitive vs non competitive inhibitor
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
Feedback inhibition
Final product of reaction binds to first enzyme's allosteric site, stopping production