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MED-103 Biology I (2024-25) > Topic 4: structure + function of macromolecules > Flashcards

Topic 4: structure + function of macromolecules Flashcards

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1
Q

Give the 4 biological macromolecules

A

1) Carbohydrates
2) Lipids
3) Protiens
4) Nucleic acids

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2
Q

Define biomolecule

A
  • Chemical molecule = structural/functional component of living organism
  • Synthesis of biomolecules mostly = C + H
  • Also O + N + S + P
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3
Q

Define polymer

A
  • Long molecule consisting of small building block = monomers
  • 3/4 classes = polymers = Carbs + Proteins + Nucleic acid
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4
Q

What are the subunits of the macromolecules?

A
  • Monosaccharides > Carbohydrates
  • Fatty acids > Lipids
  • Amino acids > Proteins
  • Nucleotides > Nucleic acid
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5
Q

Describe the condensation reaction

A
  • Dehydration reaction
  • 2 monomers bond through loss of H2O = Form polymers
  • Enzymes speed up dehydration
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6
Q

Describe the hydrolysis reaction

A
  • Reverse of condensation
  • Disassembles polymer > monomer by adding H2O
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7
Q

Describe carbohydrates

A
  • (CH2O)n
  • AKA sugars
  • Monosaccharides = simple sugars
    1) Glucose
    2) Fructose
    3) Galactose
  • Disaccharides = 2 monosaccharides
    1) Maltose
    2) Sucrose
    3) Lactose
  • Oligosaccharides = 20-30 monosaccharides
  • Polysaccharides = carb polymer
    1) Starch
    2) Glycogen
    3) Cellulose
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8
Q

Describe monosaccharides

A
  • Glucose = C6H12O6 = most common
  • Fuel for cells + raw material for building
  • Classified by = location of carbonyl group + number of carbons in skeleton
  • If C=O at end of sugar = aldose
  • If C=O middle of sugar = ketose
  • Linear but may form rings in aqueous solution
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9
Q

Describe disaccharides

A
  • Formed by condensation reaction to join 2 monosaccharides = covalent bond = glycosidic linkage
  • Glucose + glucose = maltose
  • Glucose + galactose = lactose
  • Glucose + fructose = sucrose
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10
Q

Describe polysaccharides

A
  • Have storage + structural roles
  • These are determined by monomers + position of glycosidic linkages
  • Starch + Glycogen = made of glucose + for storage
  • Cellulose + Chitin = structural
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11
Q

What are the 2 glycosidic linkages?

A

1) α-linkage = OH group of C2 same side as OH group on C1
2) β-glucose = OH group on C2 different side than C1
- α = helical
- β = linear

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12
Q

Describe starch

A
  • Storage of glucose in plants
  • Plants store excess starch in chloroplasts + amyloplasts
  • 2 polysaccharides = amylose + amylopectin
  • Amylose = 1-4 glycosidic linkage = unbranched
  • Helical due to α-linkage
  • Amylopectin = 1-4 + 1-6 glycosidic linkage = branched
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13
Q

Describe glycogen

A
  • Storage of glucose in animals
  • Animals/humans store glycogen in liver + muscle cells = cytosolic granules
  • α-glucose = helical
  • Has 1-4 + 1-6 glycosidic linkage = branched = enzyme accessible
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14
Q

Describe cellulose

A
  • Component of plant cell wall
  • Unbranched β-glucose polymer = linear
  • Humans can not digest = passes through digestive tract as insoluble fiber
  • Herbivores = symbiotic relationship with microbes in stomach to break down cellulose
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15
Q

Describe chitin

A
  • Component of exoskeleton of arthropods + fungal cell walls
  • Used to make surgical thread
  • β - glucose = linear
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16
Q

Describe lipids

A
  • Doesn’t have polymers
  • Hydrophobic = consist if hydrocarbons = non-polar covenant bonds
  • Fats + Phospholipids + Steroids
17
Q

Describe fats

A
  • Triglycerides = storage = 1 glycerol 3 fatty acids
  • Hydrophobic
  • Condensation reaction between glycerol + each fatty acid= ester linkage
  • Function = energy storage
  • Humans store fat in adipose cells = adipose tissue cushions vital organs + insulates body
18
Q

Describe fatty acids

A
  • Structure = R-COOH
  • R = long hydrocarbon chain
  • Fatty acids differ in length + number/location of double bonds
  • Saturated > no =
  • Unsaturated > 1 or more =
    SATURATED:
  • Max amount of H
  • CH3(CH2)nCOOH
  • Mostly found in animals
  • Solid at room temp = butter
  • Diet rich in saturated fats = contribute to CVD = plaque deposits
  • Directly increase LDL bound bad cholesterol
    UNSATURATED:
  • Found in plants + fish
  • Liquid at room temp = oil
  • Signals liver = take up cholesterol from blood = improve cholesterol levels
  • Reduce LDL bound bad cholesterol + maintain HDL good cholesterol
19
Q

Describe phospholipids

A
  • Have phosphate group instead of 3rd fatty acid
    1) Phosphoglyceride = glycerol + 2 fatty acid + phosphate + organic molecule
    2) Phosphospingolipids = sphingosine + 1 fatty acid + phosphate + organic molecule
  • Function = components of biological membranes
  • Amphipathic molecule = hydrophilic head + hydrophobic tail
20
Q

Give some common membrane phospholipids

A
  • Phosphatidyl-choline = glycerol + choline
  • Phosphatidyl-ethanolamine = glycerol + ethanolamine
  • Phosphatidyl-serine = glycerol + serine
  • Phosphatidyl-inositol = glycerol + inositol
  • Sphingomyelin = sphingosine + choline
21
Q

Describe the bilayer

A
  • When phospholipids exposed to water = assemble in bilayer = hydrophobic tails interior and hydrophilic heads exterior
  • Found in cell membranes = main component
22
Q

Describe steroids

A
  • Lipids made of carbon skeleton of 4 fused rings
  • Cholesterol = steroid in animal cell membrane + precursor for hormones
  • Steroid hormones = androgens + estrogens
23
Q

Describe health risks of cholestrol

A
  • High level in blood = CVD
  • In blood bound to lipoproteins = low density / high density
  • Lipoproteins recognized by receptor on plasma of liver cells = cholesterol released into liver via receptor-mediated endocytosis
  • HDL bound cholesterol = good = protein > cholesterol = travels fast in blood + deposited directly to liver
  • LDL bound cholesterol = bad = cholesterol > protein = travels slow in blood = leaves pieces around = plaque
24
Q

Describe proteins

A
  • 50% dry mass of cells
  • Functions= structural support + storage + transport + cellular communication + movement + defense against foreign substances
  • Polypeptide = polymer of amino acids
  • Protein = 1> polypeptides = each has unique linear sequence of amino acids
  • Amino acids linked by covalent bond = peptide bond between carbonyl of 1 + amino of other via condensation reaction
25
Q

Define enzyme

A
  • Protein that acts as catalyst = speed up chemical reactions
26
Q

Describe amino acids

A

H
NH3-C-COOH
R
- Have carboxyl group + amino group
- Different properties due to differing R groups
- 3 types = non-polar + polar + electrically charged

27
Q

What are the non-polar amino acids?

A
  • Gly
  • Ala
  • Val
  • Leu
  • Ile
  • Met
  • Phe
  • Trp
  • Pro
28
Q

What are the polar amino acids?

A
  • Ser
  • Thr
  • Cys
  • Tyr
  • Asn
  • Gln
29
Q

What are the electrically charged amino acids?

A

ACIDIC
- Asp
- Glu
BASIC
- Lys
- Arg
- His

30
Q

Describe protein structure + function

A
  • Machines can determine structure = X-ray crystallography
  • Functional proteins contain more than 1 polypeptide
  • Sequence of amino = 3D structure = function
  • Primary structure = unique sequence of aminos
  • Secondary structure = either coiling / folding of polypeptide chain = α-helices / β-pleated sheets
  • Tertiary structure = 3D structure determined by interaction in R group
  • Quaternary structure = multiple polypeptides bind
31
Q

What types of interactions take place in the tertiary structure?

A
  • Disulphide bonds = between 2 S in S-H groups in R group
  • H-bonds
  • Van der Waals
  • Ionic
  • Hydrophobic
32
Q

Explain protein folding chaperones

A
  • Proteins go through several intermediate states = stable conformation
  • Chaperonins = proteins that assist + maintain folding of proteins
  • Location = cytosol + mitochondria + ER
33
Q

Explain sickle cell disease

A
  • Slight change in primary structure = affects protein structure + ability to function
  • Inherited blood disorder
  • Due to substitution of a single amino in haemoglobin in RBC
  • Shape deformed = unable to carry oxygen
34
Q

Describe haemoglobin

A
  • Globular protein = 4 polypeptides = 2 alpha + 2 beta
35
Q

Explain protein conformation

A
  • Conformation depends on physical + chemical environment of protein
  • Denature = loss of conformation due to unraveling = loss of function = biologically in active
    DENATURE FACTORS
  • pH change
  • Salt concentration change
  • Temp change
36
Q

Describe nucleic acids

A
  • Store + transmit hereditary info
  • Nucleotide structure = phosphate group + pentose sugar + nitrogenous base
  • Nitrogenous bases = A G C T/U
  • Sugars = deoxyribose/ ribose
  • Polymer = polynucleotide = goes from 5’ to 3’
  • Connected with a phosphodiester bond = OH 3’ + phosphate 5’
    2 TYPES:
    1) Deoxyribonucleic acid = DNA
  • Stores info for protein synthesis
  • Directs RNA synthesis
  • Directs protein synthesis through mRNA
    2) Ribonucleic acid = RNA
37
Q

Define gene

A
  • Unit of inheritance
  • Amino acid sequence for polypeptide
  • Made of DNA = nucleic acid
38
Q

Describe a DNA double helix

A
  • 2 anti-parallel polynucleotide strands = double helix
  • Strands run in opposite directions = 5’>3’ + 3’>5’
  • Held together by H-bonds between bases
  • Sugar+phosphate backbone
  • Complementary base pairs = AT + CG
39
Q

Explain DNA replication

A
  • Copy all DNA molecules into a 2nd set
  • Required before cell division
  • 2 strands separate = H-bonds break = each stand is template for complementary copy

MED-103 Biology I (2024-25) (6 decks)

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