Bio 20 Flashcards

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1
Q

metabolism

A

all of the reactions which occur within our bodies (how quickly for food to become energy

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2
Q

organic molecules

A

carbon based molecules

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3
Q

organic molecule’s function

A

energy storage

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4
Q

carbohydrates

A

our body’s most important source of energy, plants

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5
Q

3 elements in carbohydrates

A

carbon, hydrogen, oxygen (“CHO”)

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6
Q

C, H, O occurs in a __:__:__ ratio in glucose

A

1:2:1 ratio in glucose

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7
Q

the number of carbons determine

A

the size of the molecule

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8
Q

to identify a sugar it ends with a “______”

A

“-ose”

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9
Q

Monosaccharide

A

simple sugars (one molecule)

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10
Q

isomers

A

same molecular formula (C6H12O6) bud different structural arrangement

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11
Q

disaccharides

A

combination of two monosaccharides by the removal of a water molecule
ex. sucrose, lactose, maltose

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12
Q

dehydration synthesis

A

removal of water molecules

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13
Q

polysaccharide

A

union of many monosaccharides

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14
Q

polysaccharide: Starch

A

plant polysaccharide

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15
Q

polysaccharide: cellulose

A

building block of plant cell walls

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16
Q

polysaccharide: glycogen

A

animal carbohydrate storage form, stored in liver and muscles

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17
Q

lipids (fats)

A

non-polar compounds that are insoluble in polar solvents like water, fats float,

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18
Q

lipids function

A

help store energy

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19
Q

what are lipids made of

A

glycerol and fatty acids

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20
Q

triglycerides are formed by

A

glycerol and fatty acids

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21
Q

triglycerides have ______ and ______

A

fats from animals (solid) at room temperature
Oils from plants (liquid) at room temperature

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22
Q

animal fat

A

saturated fats that have single covalent bonds

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23
Q

plant fats

A

polyunsaturated (double covalent bonds)

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24
Q

saturated fats

A

more stable, difficult to break down, solid, ex. animal

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25
Q

unsaturated fats

A

liquid

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26
Q

phospholipids

A

add a phosphate molecule to a lipid

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27
Q

waxes

A

long, stable molecules, waterproofing

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28
Q

proteins

A

structural components

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29
Q

what are proteins made of

A

C,H,O and nitrogen

30
Q

Amino acids

A

building blocks of protein

31
Q

Amino Groups

A

NH2

32
Q

Acid Group

A

COOH

33
Q

dehydration synthesis

A

a change in single amino acid can alter the protein, proteins join together form a peptide bond through dehydration synthesis

34
Q

polypeptide

A

when many peptide bond to make ______

35
Q

how many amino acids are there

A

20

36
Q

true/false, all amino acids can be made by the body

A

false

37
Q

proteins can change due to

A

temperature, ph, heavy metals

38
Q

denature

A

temporary protein change

39
Q

coagulation

A

a permanent protein change

40
Q

exothermic reaction

A

reactions that have a net loss of energy in the form of light, heat, or sound

41
Q

initial energy

A

required to start raction
known as activation energy

42
Q

endothermic reaction

A

requires the constant addition of energy from an external source

43
Q

does products have more energy than reactants?

A

yes
ex. photosynthesis

44
Q

catabolism

A

breaking down of complex molecules to more smaller one. ex. glycogen to glucose to use in the blood stream

45
Q

anabolism

A

simple molecules, complex structures
ex. glucose to glycogen

46
Q

catabolism

A

breaking down complex molecules to smaller ones. ex. glycogen to glucose to use in the bloodstream

47
Q

catalysts

A

chemicals that control the speed of chemical reactions without altering the products formed, can be used again and again

48
Q

enzymes

A

globular protein catalysis found within living organisms

49
Q

enzymes permit low temperature reactions by

A

reducing the reaction’s activation energy

50
Q

enzymes end in the surfix?

A

“ose”

51
Q

orient molecules for?

A

interaction

52
Q

substrate

A

molecules that the enzymes act upon, changes into a product for the reaction

53
Q

how does enzymes increase the possibility of reaction

A

by bring reactants together

54
Q

active site

A

area of the enzyme that combines with the substrate

55
Q

The “lock and key” model is proposed by

A

Emil Fischer

56
Q

“lock and key”

A

describes enzyme-substrate complex

57
Q

induced fit model

A

theory modifies, suggest the actual shape of the active sight is modifies

58
Q

cofactors

A

inorganic molecules that help enzymes to bind with substrate molecules

59
Q

coenzymes

A

organic molecules synthesized from vitamins that help enzymes to bind with substrate molecules

60
Q

can coenzymes and cofactors work with more than one kind of enzyme

A

yes

61
Q

factors effecting enzyme reactions

A
  1. competitive inhibitors
  2. non-competitive inhibitors
  3. feedback inhibition
  4. temperature
  5. pH
  6. substrate or enzymes concentration
62
Q

competitive inhibitors

A

molecules with shapes similar to the substrate and will compete with the substrate fir the active site

63
Q

non-competitive inhibitors

A

a substance that binds to a site other than active site, changes shape of active site, adding more substrate has no effect

64
Q

feedback inhibition

A

in a metabolic pathway by the final product of the pathway, slows the reaction rate, and combines with the enzyme at a regulatory site, changing enzyme shape

65
Q

temperature

A

heat will increase reaction rates as the molecules involved move faster and collide more often

66
Q

what does temperature peak at to have enzyme denature

A

37 degrees Celcius, higher temperatures change active site

67
Q

pH

A

each enzyme functions within a certain ph scale

68
Q

what can pH disrupt

A

the hydrogen bonds between the amino acid group, changing enzyme shape

69
Q

what can stomach enzymes function to

A

pH 9

70
Q

substrate concentration

A

the greater the # of substrate exceeds the number of available enzymes, the reaction rate will level off