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BIOL 107 FINAL EXAM > Lecture #2 - Chemical bonds and Macromolecules > Flashcards

Lecture #2 - Chemical bonds and Macromolecules Flashcards

1
Q

Organic Molecules

A
  • contain C-H, no dipoles
  • C is the backbone of organic molecules
  • C is weakly electronegative
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2
Q

Why is life carbon based?

A
  • C can bond to 4 other atoms
  • can form C-C chains
  • can form double and triple bonds
  • these all allow for molecular diversity
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3
Q

define monomer

A
  • “single unit”
  • building block of a polymer
  • eg. nucleotide
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4
Q

define polymer

A
  • “multiple unit”
  • chain of monomers composed of similar or identical subunits
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5
Q

why are polymers more biologically important than monomers?

A
  • allow for variations
    eg. proteins = 20 a.a., DNA+ 4 nucleotides
  • in combination, the variety is infinite
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6
Q

Synthesis- condensation rxns/dehydration

A
  • add monomers into a chain by catalyzing covalent bonds
  • water is a product
  • requires energy
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7
Q

breakdown - hydrolysis rxns

A
  • cleavage of covalent bonds b/w monomers
  • water is a reactant
  • release energy
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8
Q

What is the function and structure of a carbohydrate/polysaccharide/sugar

A
  • energy store
  • gives cell strucutre
  • cell-cell recognition
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9
Q

what is a glycosidic bond?

A

a covalent bond formed between monosaccharides

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10
Q

monosaccharide example: glucose

A

C6H12O6
- main energy source in all cells
- multiple chains of CH2O
- can either be linear or ring shaped
- alpha form is when the OH group is at the bottom, ring shape dominates in the cell
- alpha form is less common irl but more widely used

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11
Q

Disaccharides example: sucrose

A
  • formed from the covalent (glycosidic) bond b/w glucose and fructose
  • uses a dehydration rxn to join the two
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12
Q

polysacc eg: starch

A
  • nutritional polysacc
  • polymer of alpha glucose
  • contains alpha 1-4 glycosidic bonds
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13
Q

polysacc eg: glycogen

A
  • nutritional polysacc
  • polymers of alpha glucose, connected by alpha 1-4 glycosidic bonds
  • highly branched by alpha 1-6 glycosidc bonds
  • function: energy storage in animals in muscle and liver
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14
Q

polysacc eg: cellulose

A
  • structureal polysacc
  • function: provide structure to plant cell walls
  • contains beta 1-4 glycosidic bonds
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15
Q

polysacc eg: chitin

A
  • structural polysacc
  • polymer of monosacc
  • found in insect exoskeleton and fungi
  • peptidoglycan - function: structure to bacterial cell wall
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16
Q

Lips/fats - classification, function and structure

A
  • not true polymers- not joined into polymers by covalent bonds
  • hydrophobic: non-polar molecules made of mostly H-C
  • non-polar lipids aggregate away from water
  • they are single chains of mostly HC with a COOH end and is usually 16-18C long
  • can esterify to a 3C glycerol backbone
17
Q

fats/lips - triglyceride: saturated or unsaturated

A
  • function: energy storage in animals
  • it can be saturated or unsaturated
  • sat: all c-c single bond, solid at room temp, linear fatty acids
  • unsat: presence of C=C creates a kink in fatty acid tail, liquid at room temp
18
Q

fats/lips - phospholipids

A
  • structural component of biological membrane
  • functions in the cell membrane
  • 2HC chains attached to a glycerol backbone via ester linkages with a phosphate group attached to the 3rd glycerol
  • phospholipids are amphipathic = both hydrophobic and hydrophilic domains
  • hydrophilic head, hydrophobic tails
19
Q

fats/lips - steroids

A
  • class of lipids based on cholesterol
  • slighty amphipathic
  • planar/flat
    2 major functions:
    1. hormones eg.testosterone
    2. membrane structure: in animals cholesterol in remembrance modulates membrane fluidity
20
Q

Proteins

A
  • polymers of a.a
  • involved in every biological task
  • 20 biologically relevant a.a
21
Q

Draw a protein, indicate the directionally, and the types of variable groups

A

n-c directionality
variable groups:
- non-polar
- polar uncharged
- polar charged
- polar charged basic

22
Q

Structure of protiens

A
  • function in 3D
  • synthesized as linear polypeptides
  • product of dehydration reactions
23
Q

what is a peptide bond?

A

bond formed between a.a, it links them together to make a protein

24
Q

Primary sequence

A
  • polymer of a.a
  • sequence is determined by the DNA sequence of a gene
  • primary sequence dictates fold and folding dictates function
25
Q

secondary sequence

A
  • local folding of a.a chain into an alpha helix or beta sheet
  • R groups drive the folding, they don’t stabilize it
  • stabilized by H-bonds b/w a.a backbones
26
Q

tertiary sequence

A
  • hydrophobic R groups bury into the middle of protein to aggregate away from water
  • R group interactions stabilize the structure
    1. covalent - disulfide bridge, very strong but rare
    2. ionic bonds - b/w oppositely charged R groups
    3. hydrogen bonds - b/w polar uncharged a.a
    4. hydrophobic interactions - b/w non-polar a.a
27
Q

quaternary sequence

A
  • some proteins function as multisubunit complexes
  • complex is stabilized by same R group interactions as tertiary sequence
  • eg ribosomes
28
Q

what are chaperones?

A
  • proteins that assists in folding other proteins
  • proper folding is essential for proper function
    there are many diseases of protein folding
  • misfolded proteins are usually degraded
  • if not degraded they can : refold with chaperones =good or aggregate = bad
29
Q

Nucleic Acids( DNA/RNA) function

A

function:
- store and transmit hereditary information
- RNA tramits within cells
- DNA transmits b/w cells

30
Q

DNA

A
  • molecule of heredity
  • polymer of nucleotides (ntds)
  • deoxyribonucleotides
31
Q

RNA

A
  • polymer of ribonucleotides
    many fxns:
  • info transmission
  • translation
  • splicing
  • gene regulation
32
Q

draw the basic structure of a nucleotide, define what each carbon is for, identify the directionality and the base stacking

A
  1. Pi = inorganic PO4-
  2. SC = sugar = ribose
  3. nitrogenous base

c1 = attaches to the NB
c2 = if DNA - just H group, if RNA - OH group
c3 = OH group
c4 = nothing boring
c5 = Pi attachment

5’ -> 3’ directionality
- hydrophobic base stack interactions stabilizes double helix

33
Q

pyrimidines and purines and the complementary base pairing rule

A

A=T
G=- C
purine always pairs with a pyrimidine, this maintains the diameter of the helix
- pyrimidines = single ringed bases: cytosine, thymine, uracil
- purines = double ringed bases: adenine and guanine

34
Q

What is a phosphodiester bond?

A
  • monomers joined in a sugar-phosphate backbone
35
Q

Why is RNA single stranded?

A
  • 2’ OH makes helix more open
  • 2’ OH makes RNA more reactive so it can base pair with: itself, other RNA and DNA

BIOL 107 FINAL EXAM (9 decks)

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