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Bio 107 topic 3 Flashcards

1
Q

Macromolecules

A

large complex molecules

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2
Q

What are the 4 classes of macromolecules?

A
  • carbohydrates
  • lipids (not a polymer)
  • nucleic acids
  • proteins
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3
Q

Polymers

A

molecules consisting of many similar or identical building blocks linked together by covalent bonds

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4
Q

Monomers

A

small molecule used as a building block in a polymer

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5
Q

Synthesis of polymers (dehydration)

A
  • covalent bond form between monomers
  • water molecule is lost
  • requires energy
  • requires enzymes
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6
Q

Degradation of polymers (hydrolysis)

A
  • breaks covalent bond between 2 monomers
  • adds an H20
  • releases energy
  • requires enzymes
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7
Q

Sugars

A
  • source of energy (from hydrolysis)
  • source of carbon to make other molecules
  • structural components of the cell
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8
Q

Monosaccharide (monomer)

A
  • simple sugar
  • one carbonyl and many hydroxyls per carbon
  • forms rings in solution because cytoplasm is water
  • easy to dissolve
  • joined by a glycosidic linkage to form polymers (covalent bond formed by dehydration reaction)
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9
Q

What causes variation in monosaccharides?

A
  • length of skeleton
  • position of carbonyl group
  • spatial arrangement of functional groups
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10
Q

What is a carbohydrate?

A
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11
Q

Aldose

A

carbonyl on end C (aldehyde)

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12
Q

Ketose

A

carbonyl on a middle C (ketone)

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13
Q

Enantiomers

A

mirror images of each other

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14
Q

Polysaccharide

A

more than two monosaccharides joined by glycosidic linkages

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15
Q

What are the functions of polysaccharides?

A
  • storage
  • structure
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16
Q

What are the storage polysaccharides?

A
  • starch
  • glycogen
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17
Q

Starch

A

storage polysaccharide
- only in plants
- polymers of glucose monomers joined by α-1,4-glycosidic bonds
- helical structure
ex. amylose

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18
Q

Glycogen

A
  • found in animal liver and muscle cells and bacteria
  • glucose polymer with α-1,4-glycosidic bonds
  • helical structure
  • branched
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19
Q

What are the structural polysaccharides?

A
  • cellulose
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20
Q

Cellulose

A
  • found in plant cell walls
  • polymer of glucose with β-1,4-glycosidic linkages
  • unbranched, linear structure
  • forms strong bundles
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21
Q

Types of lipids

A
  • fats
  • phospholipids
  • sterols
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22
Q

Lipids

A
  • partially hydrophobic
  • not a polymer
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23
Q

Fats

A

type of lipid
- energy source
- insulation
- protection

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24
Q

What are the two components of fats?

A

glycerol (3 carbons and hydroxyls)
fatty acid (hydrocarbon chain and one carboxyl on one end)

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25
Triaglycerol
1 glycerol and 3 fatty acids - attached by ester linkages - formed by dehydration reactions
26
Phospholipids
type of lipid - main component of cell membranes - hydrophilic head and hydrophobic tail (amphithatic) - similar to fat except 3rd carbon is attached to phosphate group - spontaneously assemble into bilayers
27
Sterols
type of lipid - cell membrane, signalling molecules - not in plants - non polar - carbon skeleton of 4 fused rings ex. cholesterol
28
Saturated fatty acids
- no double bonds - straight molecules that pack close together - solid at RT ex. red meat and butter
29
Unsaturated fatty acids
- one or more double bonds - bend at double bond and can't pack close together - liquid at RT ex. oils, fish plants
30
Types of unsaturated fatty acids
cis and trans
31
Cis
same side, natural, bent molecule
32
Trans
opposite sides, unnatural, straight molecules
33
Why is adding trans fats to foods bad for our health?
- unnatural - cannot be digested properly - clog arteries - cause inflammatory responses
34
DNA
- contains all instructions for cell structure and function - directs its own replication - directs RNA synthesis
35
RNA
- carries information in our cells - essential for protein synthesis - exists as a single strand - unique shape due to internal base pairing
36
Nucleotide (monomer)
- made of three parts (nitrogenous base, five carbon sugar, 3 phosphate groups) - in ribose OH is attached to sugar and just H in deoxyribose
37
Nucleic acid (polymer)
chain of nucleotides - attached by a phosphodiester linkage - 3' -OH of one nucleotide attached to 5'-phosphate of the next nucleotide - directional molecules
38
Phosphodiester bonds
bonds that connect the nucleotide, specifically the phosphate group
39
What does the fixed width of a double helix mean?
Purine must pair with pyrimidine - purine + purine= too wide - pyrimidine + pyrimidine = too narrow
40
Purine
A + G
41
Pyrimidine
C + T
42
How are the strands of DNA connected?
H-bonds between bases - 2 contacts for A + T - 3 contacts for C + G (stronger)
43
Base pairing for DNA/RNA
DNA: A+T, C+G RNA: A+U, C+G
44
Why can DNA dentaure?
H-bonds are weak and increased molecular motion caused by heat will break them. Two strands come apart. Covalent bonds don't break so denatured DNA exists as single strands by phosphodiester bonds
45
Types of polypeptides
- hemoglobin - collagen - insulin
46
Functions of polypeptides
- enzymes - transport proteins - hormones - receptors - motor proteins - structural proteins
47
Four classes of amino acids
- non polar - polar, uncharged - polar + charged - polar - charged
48
Amino acid (monomer)
- amino group - carboxyl group - central carbon - R group= 20 dif structures - ionized in the cell
49
Polypeptide (polymer)
linear chain of amino acids - covalent bond called peptide bond - directional molecules
50
Peptide bond
carboxyl group of one AA covalently joined amino group of the next AA - formed by dehydration reaction
51
Protein
polypeptide that has been folded into a unique 3d structure
52
4 levels of protein structure
1. Primary structure 2. Secondary structure 3. Tertiary structure 4. Quaternary structure
53
Primary structure of protein
- unique order of amino acids in a polypeptide - bond type: peptide covalent - determined by DNA sequence
54
Secondary structure of protein
- repetitive coiling or folding of protein - bond type: H-bond in polypeptide backbone not sidechains ( between amino group of one AA and carboxyl group of another AA). Either alpha helix or beta sheet
55
Alpha (α) helix
- Repetitive coiling - H-bonds between every 4th amino acid in helix
56
Beta (β) sheet
- Repetitive folding - 2 regions of peptide chain lie side-by-side and are connected by H-bonds
57
Tertiary
- overall shape of single polypeptide - due to interactions between side chains (H-bonds, ionic bonds, hydrophobic interactions, disulfide bond)
58
Hydrophobic interactions
- non polar side chains aggregate inside protein and exclude water - polar side chains exposed on the protein surface interact with water
59
Disulfide bond
covalent bond between sulfhydryl groups in the side chains of cysteine (AA)
60
Quaternary
- multiple polypeptides folded together (has its own 1, 2, 3 structure) - stabilized by the same 4 types of side chain interaction as 3 - protein may contain multiple copies of the same polypeptide or several different polypeptides
61
Protein functions
- enzymes - transport proteins - hormones - receptors - motor proteins - structural proteins - storage proteins - defensive proteins
62
What directs a protein's function?
its shape (different order of amino acids) - changes to the primary structure can alter or eliminate function
63
Conservative change
change in primary sequence where the new AA has the same properties as old AA - similar bonds can form - change has minimal effect on function
64
Non-conservative change
change in primary sequence where new AA has different properties than old AA - different bonds can form - protein function is affected
65
Denaturation
when a protein unfolds and loses its normal shape - causes a loss of function
66
What can cause denaturation?
- high temps - change in pH - organic solvents (alters hydrophobic interactions) - chemicals that disrupt bonds (reducing agents break disulfide bonds)

Bio 107 (5 decks)

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