Bio 20 Flashcards

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
unsaturated fats
liquid
26
phospholipids
add a phosphate molecule to a lipid
27
waxes
long, stable molecules, waterproofing
28
proteins
structural components
29
what are proteins made of
C,H,O and nitrogen
30
Amino acids
building blocks of protein
31
Amino Groups
NH2
32
Acid Group
COOH
33
dehydration synthesis
a change in single amino acid can alter the protein, proteins join together form a peptide bond through dehydration synthesis
34
polypeptide
when many peptide bond to make ______
35
how many amino acids are there
20
36
true/false, all amino acids can be made by the body
false
37
proteins can change due to
temperature, ph, heavy metals
38
denature
temporary protein change
39
coagulation
a permanent protein change
40
exothermic reaction
reactions that have a net loss of energy in the form of light, heat, or sound
41
initial energy
required to start raction known as activation energy
42
endothermic reaction
requires the constant addition of energy from an external source
43
does products have more energy than reactants?
yes ex. photosynthesis
44
catabolism
breaking down of complex molecules to more smaller one. ex. glycogen to glucose to use in the blood stream
45
anabolism
simple molecules, complex structures ex. glucose to glycogen
46
catabolism
breaking down complex molecules to smaller ones. ex. glycogen to glucose to use in the bloodstream
47
catalysts
chemicals that control the speed of chemical reactions without altering the products formed, can be used again and again
48
enzymes
globular protein catalysis found within living organisms
49
enzymes permit low temperature reactions by
reducing the reaction's activation energy
50
enzymes end in the surfix?
"ose"
51
orient molecules for?
interaction
52
substrate
molecules that the enzymes act upon, changes into a product for the reaction
53
how does enzymes increase the possibility of reaction
by bring reactants together
54
active site
area of the enzyme that combines with the substrate
55
The "lock and key" model is proposed by
Emil Fischer
56
"lock and key"
describes enzyme-substrate complex
57
induced fit model
theory modifies, suggest the actual shape of the active sight is modifies
58
cofactors
inorganic molecules that help enzymes to bind with substrate molecules
59
coenzymes
organic molecules synthesized from vitamins that help enzymes to bind with substrate molecules
60
can coenzymes and cofactors work with more than one kind of enzyme
yes
61
factors effecting enzyme reactions
1. competitive inhibitors 2. non-competitive inhibitors 3. feedback inhibition 4. temperature 5. pH 6. substrate or enzymes concentration
62
competitive inhibitors
molecules with shapes similar to the substrate and will compete with the substrate fir the active site
63
non-competitive inhibitors
a substance that binds to a site other than active site, changes shape of active site, adding more substrate has no effect
64
feedback inhibition
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
temperature
heat will increase reaction rates as the molecules involved move faster and collide more often
66
what does temperature peak at to have enzyme denature
37 degrees Celcius, higher temperatures change active site
67
pH
each enzyme functions within a certain ph scale
68
what can pH disrupt
the hydrogen bonds between the amino acid group, changing enzyme shape
69
what can stomach enzymes function to
pH 9
70
substrate concentration
the greater the # of substrate exceeds the number of available enzymes, the reaction rate will level off