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biol 314 > chapter 3.1 macromolecules > Flashcards

chapter 3.1 macromolecules Flashcards

1
Q

chemical composition of the cell

A
  • dry weight of e.coli: 2.8 x 10^-13 grams
  • total weight (70% water): 9.5 x 10^-13 grams
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2
Q

chemical composition protein

A

50% dry weight
(there are 2000 different types of proteins)

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3
Q

FUNCTIONAL GROUPS

A

MEMORIZE

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4
Q

covalent bonds

A

bonds in which electrons are shared between atoms (these don’t break even when H bonds are broken by boiling conditions

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5
Q

hydrogen bonds (weak)

A

hydrogen bonds form between H and other electronegative elements (O or N)

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6
Q

other weak bonds

A

van der waals and hydrophobic interactions

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7
Q

GCAT

A
  • takes more energy to separate CG than AT
  • AT is 2 bonds
  • CG is 3 bonds
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8
Q

four classes of macromolecules

A
  • polysaccharides
  • lipids (fats)
  • nucleic acids
  • proteins
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9
Q

carbohydrates

A

CH2O (1:2:1 ratio)
- most relevant carbs contains 4,5,6,7, carbon atoms
- most relevant carbs are D-form sugars
- optically active (chirality)
- OH group of next to last carbon determines chirality of molecule

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10
Q

D sugars

A
  • right rotating
  • most natural sugars are D
  • our enzymes only work with D, not L
  • D glucose will have more OH groups on the right, L on left
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11
Q

polysaccharides

A
  • high molecular weight carbs containing monomeric units
  • can be linked to proteins or lipid molecules to form glycoproteins and glycoproteins
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12
Q

polysaccharides
α-glycosidic bond

A
  • right side up H
  • carbon and energy reserves in bacteria, plants, and animals
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13
Q

polysaccharides
β-glycosidic bond

A
  • right side down H
    often used as structural components of cells (cellulose)
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14
Q

lipids

A
  • fatty acids bound to glycerol
  • contain hydrophobic and hydrophilic components
  • principle component of membranes
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15
Q

lipids - bonds

A
  • every C attached to a H is saturated (single bonds outside of func group)
  • if H is removed, double bond will form (unsaturated)
  • more than one double bond is polyunsaturated
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16
Q

lipid structure

A

bacteria is same as eukarya, but different for archaea

17
Q

phospholipid membrane

A
  • one molecule
  • proteins mobile in hydrophobic region of phospholipid membrane, BUT do not leave that area
18
Q

nucleic acid polymers

A
  • DNA is a polymer of deoxyribonucleic acid
  • RNA is polymer of ribonucleic acid
19
Q

nucleic acid structure

A
  • ribose or deoxyribose sugar
  • nitrogenous base
  • phosphate group
20
Q

bases of nucleic acids

A
  • purine or pyrimidine
  • purines have two rings (A and G)
  • pyrimidines have one ring (C, T, U)
21
Q

nucleic acid configuration

A

3’ to 5’ configuration via phosphodiester linkage, results in primary structure of nucleic acid

22
Q

nucleic acid base bonds

A

H bond to one another in a specific manner
- A to T, or U
- G to C

23
Q

secondary structure in RNA

A

when H bonds form between bases within the chain

24
Q

ribose vs deoxyribose (OH/H)

A
  • ribose has OH on 2’
  • deoxyribose has no OH, just H on 2’
25
Q

3 rules of biochemistry

A
  1. biochemistry is backwards
  2. biochemistry does not happen in the absence of water
  3. biochemistry is STUPID
26
Q

amino acids

A
  • monomeric units of protein and polypeptides
  • joined to each other in a peptide linkage
  • 21 commonly occurring amino acids
  • optically active
  • L-form commonly used
27
Q

proteins (primary and secondary structure)

A
  • juxtaposition of α-carbon R groups dictates the primary structure of a protein (the amino acid sequence)
  • twists and folds in the linear sequence caused by H bonding determine the Secondary Structure of the protein
28
Q

secondary structure of protein

A

α- helix
β- pleated sheet

29
Q

we sequence the DNA that codes the protein

A

not the actual protein itself

30
Q

primary struc

A

coded in the DNA

31
Q

secondary struc

A

interaction within a change between amino acids

32
Q

all proteins are peptide, not all peptides are proteins

A
  • may need more than one peptide
  • 1 gene (amino acid chain) = 1 peptide (single stranded)
  • protein is the finished product (1 protein = 1 OR more peptides)
33
Q

tertiary structure of a protein

A

results from further folding of secondary structure and is “cemented” by the covalent bridging of different sections of the chain by disulfide linkages

34
Q

quaternary structure

A

results when one or more peptide chains interact via strong or weak molecular bonds

35
Q

denaturation of proteins

A

occur when bonds conferring secondary, tertiary, or quaternary structure are broken either chemically or by heat or radiation

biol 314 (5 decks)

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