Chapter 3- Macromolecules/ biomolecules CLASS 1 Flashcards

(58 cards)

1
Q

4 macromolecules

A
  • Proteins
  • Carbs
  • Lipids
  • Nucleic Acids
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2
Q

Macromolecules made from_________

A
  • Polymers; large molecules made from repeating small units called monomers
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3
Q

Enzymes that make macromolecules___________

A

Polymerases

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4
Q

Reactions to make macromolecules_________

A

Polymerization

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5
Q

Dehydration synthesis/ Condensation

A
  • removing water
  • go from monomers to polymers
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6
Q

Hydrolysis

A
  • adding water
  • break polymers into monomers
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7
Q

Protein monomers

A
  • made of aa linked to make polymers
  • 20 types
  • sequence of aa is what makes each protein unique and able to fulfill the role
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8
Q

General struc/ parts of aa

A
  • alpha amino/ amine group
  • a carboxyl group/ acid group
  • tetrahedral a carbon
    ^^^ backbone
  • r group/ side chain- unique feature for each aa. What distinguishes the physical and chem properties all the types of aa
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9
Q

Peptide Bonds/ Amide bond

A
  • link aa together by peptide bonds (PB)
  • formed bw the carboxyl group of one aa and the amino group of another aa
  • hydrolysis rxn; loss of water
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10
Q

backbone polypeptide pattern

A

N-C-C-N-C-C

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11
Q

individual aa

A

Residue

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12
Q

Polypeptide synthesis direction___

A
  • amino terminus (N terminus) to carboxyl terminus (C terminus)
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13
Q

Proteolysis/ Proteolytic cleavage

A
  • hydrolysis of a protein by another a protein
  • cleavage by of a peptide bond done by proteases
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14
Q

Disulphide bonds

A
  • Cystine
  • has reactive thiol (sulfhydryl, SH) side chain
  • thiol of one cys reacts with the thiol of another cys to produce a covalent sulfur-sulfur bond
  • form bw cys on same polypeptide chain or on diff polypeptide chains
  • stabilizes protein tertiary structure
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15
Q

Struc- func relationship

A
  • in proteins
  • structure of protein dictates the func
  • fold polypeptide into 3D structure is required to make protein function
  • improperly folded or denatured proteins have no function
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16
Q

denaturation

A
  • disruption of the protein shape without breaking any peptide bonds
  • unfolding of the protein/ not proper folding
  • done by Urea, extreme pH, extreme temp, change in salt concentration (tonicity)
  • does not affect the primary struc, but does for 2,3,4
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17
Q

Primary Structure

A
  • simplest level
  • aa seq/ bonded order
  • no folding
  • linear ordering
  • bonds involved: peptide bonds
  • dictates how it folds/ tertiary struc
  • seq of aa it what makes each protein unique
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18
Q

Secondary Structure

A
  • initial folding of polypeptide chain into shapes
  • Bonds involved; Hydrogen bonds bw backbone NH (amino) and CO (carboxyl) groups
  • 2 common forms; a helix and b- pleated sheets
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19
Q

2 types B sheets

A
  1. parallel; adjacent pp strands running in same direction
  2. anti parallel; adjacent pp strands running in opposite directions
  • made of extended sheets
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20
Q

charac of a helicies

A
  • right handed
  • 3.6 residues per turn
  • 5 angstorms in width
  • each aa rising 1.5 angstorms
  • have a hydrophobic and hydrophilic portion
  • coiled
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21
Q

Tertiary structure

A
  • due to side chain interactions within a polypeptide
  • interactions bw aa more distant from eachother
  • driven by: R groups interactions with eachother and with the solvent (water)
  • hydrophobic R groups fold towards the center away from water
  • hydrophilic R groups fold towards the outside, exposed to water
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22
Q

2 main types of interactions (proteins 3, 4 levels)

A
  1. covalent
    -1)non polar to non polar
    - 2)polar to polar
    - 3)acid to base (electrostatic) - hydrophilic
    1) and 2) are hydrophobic
  2. non covalent
    - 1) disulfide bonds
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23
Q

fold protein to the__________

A
  • lowest energy conformation
  • spontaneously
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24
Q

Quaternary structure

A
  • due to side chain interactions bw 2 diff polypeps
  • any 2 or more polypeps
  • highest level
    -interaction of subunits
  • stabilizing forces; van der waals, hydrogen bonds, disulfide, eletrostatic, non covalent
25
Subunit
single polypep chain
26
Carbs monomer
- monosaccarides/ simple sugar - mono chem form; Cn H2n On
27
3 common 6C monosaccharides
- glucose - fructose - galactose all have C6H12O6
28
Carbs broken down to CO2 by_____________
- oxidation (burning/ combustion) - release alot of energy - principle energy source for cellular metabolism
29
Monosaccaride+Monosaccaride=
- Disaccharide
30
3 common disaccharides
glu+glu= Maltose glu+fructose= Sucrose glu+galactose= Lactose all have C12H22O11 - bc to link monomers together it is dehydration synthesis and a H2O is removed
31
Multiple monosaccarides=
- Polysaccaride
32
Glycogen
- polysaccaride - animal glucose storage - has alpha linkages
33
Starch
- polysac - plant glucose storage - has alpha linkages
34
alpha linkages in glycogen and starch
a 1-6 a 1-4
35
Cellulose
- polysac - play a part in plant structural role - has beta linkages; humans do not have the enzymes to break these down therefore cannot get energy out of 'em
36
Func of polysaccarides/ carbs
- energy - cell surface markers (esp in unicellular organisms)
37
Func of proteins
- receptors - enzymes - cell signalling - structural roles - pumps - energy - channels - antibodies
38
Bond between monosaccharides/ sugar molecules
Glycosidic linkage - covalent bond - formed by dehydration synthesis - requires enzymatic catalyst
39
lipids monomer
hydrocarbons
40
lipids physiological roles
1. in adipose cells, triglycerides (fats) store energy 2. in cellular membranes phospholipids are a barrier 3. Cholesterol bb for steroid hormones and mem fluidity
41
Lipids cardinal charac________
- hydrophobic - C-C bonds and C-H bonds are non polar
42
Fatty Acid
- 14- 18 carbons, made on 2C bb - composed of negative change carboxyl group head (polar/ hydrophillic) and alkanes (hydrocarbon tail, NP/ hydrophobic)
43
saturated fatty acid
- no double bonds - solid at room temp bc not kinks in the tails and pack together - every C is fully saturated with full # of Hydrogens
44
Unsaturated fatty acid
- one or more double bonds - kinks in rail - not pack tightly together - liquid at rm temp - cis config
45
fatty acids in aq solution form
Micelle - driven by hydrophobic interaction
46
Triglycerides
- made of 1 glycerol backbone and 3 fatty acids - storage form of fatty acids ^ is a fat - dehydration synthesis; loosing 3 waters - formed by esterification; held by ester links
47
Why is triglycerides good for storage/ why more efficient energy storage than carbs
- more packing; doesnt attract water; no water weight (jello analogy) - oxidation/ burning gives more energy than carbs - primary energy storage
48
lipases
- break down lipids back into fatty acids and glycerol
49
phosphlipids
- are a diacylglyerol - amphipathic; bc has a polar and non polar portion - phosphate head; polar bc of neg charge - 2 fatty acid tails; non polar - when in aq solution get spontaneous formation of a bilayer bc of hydrophobic drive
50
terpenes built from__________
isoprene units - need at least 2 isoprenes to make a terpene - isoprene form; C5H8 - gen formular; (C5H8)n
51
monoterprenes=
- 2 isoprene units
52
sesquiterpenes=
- 3 isoprene units
53
diterprenes=
- 4 isoprene units
54
squalene=
6 isoprene units - also called triterpene - used to manufacture steroids, chol and waxes
55
increase mem fluidity by
- unsaturated - decreasing fatty acid tail length - cholesterol increases fluidity at cold temp
56
decrease me fluidity by
- saturated - increasing fatty acid tail length -cholesterol decreases fluidity at hot temps
57
Cholesterol
- 3 6C rings + 1 5C ring (tetracyclic struc) - hydrophobic - from diet or liver - keeps mem fluidity at optimum level - make steroid hormones; testosterone and estradiol - make bile salts (made by liver for lipid digestion)
58
Lipoproteins
- carry chol through the blood