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bio12 > Unit 1: biochem > Flashcards

Unit 1: biochem Flashcards

1
Q

what is an atom?

A

smallest particle of an element

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2
Q

what is an ion?

A

A positively or negatively charged atom

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3
Q

what is a molecule?

A

2 or more non-metals

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4
Q

what is a compound?

A

2 or more metals and non-metals

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5
Q

electronegativity?

A

atoms ability to attract electrons to itself

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6
Q

isotope?

A

a form of an element that differs in its number of neutrons

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7
Q

isomer?

A

A molecule that has the same composition as another , but a different arrangment of atoms

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8
Q

polymer?

A

A large molecule that is formed when monomers link together chemically in a chain. EX. starch

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9
Q

structural formula?

A

H-O-H

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10
Q

molecular formula?

A

H2O

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11
Q

structural isomers?

A

same atoms bonded differently
Ex. glucose and fructose

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12
Q

stereoisomers?

A

atoms bonded in the same way but arranged differently in 3-D space

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13
Q

what makes up 50-90% of nearly all organisms?

A

WATER!!

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14
Q

what type of covalent bond is water?

A

polar covalent(uneven sharing)

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15
Q

name the 7 unique properties of water

A
  1. Cohesion
  2. Adhesion
  3. High specific heat capacity
  4. High specific heat of vaporization
    5.density
    6.universal solvent
  5. dissociation
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16
Q

cohesion?

A

As a result of hydrogen bonding water molecules tend to stick together

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17
Q

adhesion?

A

water molecules stick to other polar molecules

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18
Q

high specific heat capacity?

A
  • water requires a large amount of energy transfer to produce a change in temperature
  • protects cells from rapid temperature change and provides a stable environment for cell reaction
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19
Q

high specific heat of vapourization

A
  • hydrogen bonding causes liquid water to absorb a lot of thermal energ and turn into water vapour
  • we dispiate body heat by evaporation of water heat to cool down(sweating)
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20
Q

density

A

ice is less dense than liquid water(ice floats) due to its expansion upon freezing

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21
Q

universal solvent

A

many compounds readily dissolve in water

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22
Q

dissociation

A

water dissociates into ions

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23
Q

About 99% of the mass of most cells are made up of?

A

H,C,N,O

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24
Q

virtually all chemicals of life are?

A

C based

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25
Q

properties of carbon

A
  1. relatively light weight
  2. can make 4 bonds
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26
Q

what are functional groups?

A

groups of atoms with characteristic properties such as:polar and hydrophillic

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27
Q

linkages?

A

show the manner in which atoms of functiona; groups bond together in a molecule.

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28
Q

most important energy source for the body?

A

carbohydrates

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29
Q

what is the ratio of carbohydrates

A

1:2:1

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30
Q

what are carbs composed of?

A

single sugar molecules or chains

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31
Q

saccharide?

A

sugar (mono=1, di=2, poly= many)

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32
Q

common monosaccharides

A

glucose and fructose

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33
Q

common polysaccharides?

A

starch, glycogen, and cellulose

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34
Q

storage form of carbs in plants?

A

starch

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35
Q

forms cell walls in plants

A

cellulose

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36
Q

storage form in animals

A

glycogen

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37
Q

how are disaccharides and polysaccharides formed?

A

dehydration synthesis

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38
Q

glucose + glucose

A

maltose

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39
Q

gluctose + galactose

A

lactose

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40
Q

glucose + fructose

A

sucrose

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41
Q

composed of hydrogens carbon and oxygen?

A

lipids

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42
Q

more difficult to breakdown than carbs

A

lipids

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43
Q

what has more energy lipids or carbs

A

lipids (twice as much)

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44
Q

3 groups of lipids?

A
  1. fats, oils and waxes
  2. phospolipids
  3. steroids
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45
Q

functions of lipids

A
  1. aid in vitamin absorption
  2. insulate the body
  3. protect internal organs
  4. main components of cell membrane
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46
Q

most common form of lipids

A

triglycerides and are composed of a glycerol molecule and and 3 fatty acids

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47
Q

saturated fats?

A

have single bonds between carbon atom
EX. lard and butter

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48
Q

unsaturated fats?

A

have double bonds between at least 2 carbon atoms
Ex oil

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49
Q

A unique lipid?

A

cholesterol which is used to makes hormones in your body

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50
Q

Used to build cell structures and during chemical activities

A

protein

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51
Q

what are proteins composed of

A

hydrogen, carbon, oxygen, nitrogen and sometimes sulfur

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52
Q

what are protein subunits called?

A

amino acids

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53
Q

many amino acids joined together?

A

polypeptide

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54
Q

bonds holding amino acids together

A

peptide bond

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55
Q

how many amino acids are essential and why?

A

8, our bodies cannt synthesize them and we must get them from our diet

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56
Q

fatty acid?

A

A molecule that consists of a single hydrcarbon chain with a carboxyl group at one end

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57
Q

fat

A

a lipid that is made from 2 types of molecules: fatty acid and a glycerol molecule

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58
Q

69.5% ofour cells are made up of what

A

water

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59
Q

29.5% of our cells are made up what?

A

organic molecules

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60
Q

monosaccharides?

A

simple sugars, contain either a carbonyl aldehyde or carbonyl ketone and a hydorxyl functional group.
EX. glucose

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61
Q

disaccharides

A

2 simple sugars bonded together to form a glycosidic(ether linkage)
Ex. sucrose

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62
Q

polysaccharides?

A

monosaccharide polymer composed of monosaccharide subunits held together by glycosidic linkage.
EX. chitin, amylase, starch, cellulose

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63
Q

alpha glucose?

A

the OH lies below the plane of the ring

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64
Q

beta glucose

A

the OH lies above the plane of the ring

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65
Q

% chance of being an alpha or beta glucose

A

50%

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66
Q

glycerol?

A

3 carbon chains attached to a hydroxyl group

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67
Q

fatty acids?

A

hydrocarbon chains containing a carboxl group at one end

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68
Q

lipids are produced via what

A

dehydration synthesis between the hydroxyl group on the glycerol with the carboxyl group on the fatty acid.. producing an ester linkage

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69
Q

cholesterol

A

compact hydrophobic molecule containing 4 fused hydrocarbon rings and one hydroxyl functional group

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70
Q

most common organic molecule and most diverse

A

proteins

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71
Q

how many different amino acids

A

20

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72
Q

An amino acid has

A
  1. an amino acid
  2. carboxyl group
  3. hydrogen
  4. side chain(R group)
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73
Q

All 20 amino acids differ in what?

A

R group

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74
Q

peptide bond

A

formed by the joining of the amino end of one molecule to the carboxyl end of another via dehydration synthesis

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75
Q

4 protein structures?

A

primary, secondary, tertiary, quaternary

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76
Q

primary protein structure

A

the sequence of amino acids and a change can alter the proper functioning

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77
Q

secondary?

A

coiling and folding caused by hydrogen bonding between the R groups

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78
Q

tertiary?

A

A folded individual peptide, due to more bonding or repulsion between the R groups and the polypeptide and its environment

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79
Q

what are tertiary protein structures stabilized by

A
  1. hydrogen bonds
  2. ionic bonds
  3. disulfide bridges
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80
Q

Quaternary protein structure

A

formed by the interaction of 2 or more polypeptides
Ex. hemoglobin

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81
Q

DNA and RNA are what?

A

nucleotide polymers

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82
Q

DNA

A

deoxyribonucleic acid

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83
Q

RNA

A

ribonucleic acid

84
Q

pyrimidines

A

are the nitrogenous bases with a single ring

85
Q

purines

A

nitrogenous bases with double rings

86
Q

what does RNA have that DNA doesnt

A

uracil

87
Q

phosphodiester bonds

A

hold the phosphate group of one nucleotide and the hydroxyl group attached to the number 3 carbon of the sugar on the adjacent nucleotide

88
Q

2 strands of DNA are held together by what

A

hydrogen bonds between the nitrogenous base on adjacent strands. ( can only run if one strand is upside down)

89
Q

energy?

A

ability to do work

90
Q

kinetic energy?

A

energy possessed by moving objects

91
Q

potential energy?

A

stored energy as a result of an objects position

92
Q

work?

A

the transfer of energy from one body to another

93
Q

first law of thermodynamics

A

energy cannot be created or destroyed but only converted from one form into another

94
Q

second law of thermodynamics

A

entropy(randomness/ disorder in energy or in a collection of objects),of the universe increases with any change that occurs

95
Q

exogonic(exothermic) reaction

A

chemical reaction in which chemical potential energy is LESS THAN the energy of the reactants.
Ex. energy has been released

96
Q

endergonic(endothermic) reaction

A

chemical reaction in which chemical potential energy is MORE THAN the energy of the reactants.
Ex. Energy has been absorbed

97
Q

Anabolic reaction

A
  • reactions that produce large molecules from smaller subunits
  • Energy is absorbed
  • Ex. anabolic steroids - building muscles
98
Q

Catabolic reaction

A
  • Reactions that break macromolecules into subunits
  • Energy is released
  • Ex. Digestion
99
Q

spontaneous change

A
  • occurs on its own once started
  • does not require a continuous supply of energy
  • Ex. once a match is lit it’ll continue to burn
100
Q

non-spontaneous change

A
  • cannot occur without the continual input of energy
  • Ex. a boiling pot of water will not continue to burn if you take away its heat source
101
Q

primary source of free energy in living cells

A

ATP

102
Q

what does ATP stand for

A

Adenosine TriPhosphate

103
Q

what is ATP composed of

A

the purine nitrogenous base: adenine, a ribose sugar and a chain of 3 phosphate groups

104
Q

what is ATP a collection of

A

negative charges on the phosphate chain which make the terminal phosphate highly unstable

105
Q

what type of bond is energy stored in

A

covalent bonds between the phosphates with the greatest amount of energy between the terminal and second phosphate

106
Q

what does the free energy required from the many endothermic reactions that occur within a cell come from?

A

Hydrolysis(addition of water), with the aid of the enzyme ATPase, of the terminal phosphate from the ATP molecule

107
Q

ATP + H20 yields?

A

ADP + Pi + energy

108
Q

phosphorylation

A

transfer of the phosphate group

109
Q

How much ATP does the body use each day?

A

an amount of ATP equal to its own mass every day.

110
Q

What do catabolic processes do for ATP?

A

break down molecules to release energy needed to make ATP.

111
Q

How do anabolic processes use ATP?

A

use ATP to build larger molecules from smaller ones.

112
Q

How does the body turn ADP back into ATP?

A

The body adds a phosphate to ADP using energy from breaking down food.

113
Q

name the 5 major biological reactions

A
  1. neutralization
  2. Redox
  3. hydrolysis
  4. condensation
  5. phosphorylation
114
Q

neutralization reaction?

A

the reaction of an acid and a base to produce water and a salt
Ex. NaOH + HCl -> H2O + NaCl

115
Q

what’s a buffer

A

made up of a weak acid and its salt or a weak base and its salt.
- resists pH changes by shifting equilibrium

116
Q

human blood pH

A

7.4

117
Q

redox (oxidation-reduction)

A

reactions involving a transfer of one or more electron from one one to another

118
Q

oxidation

A

loss of electrons

119
Q

reduction

A

gain of electrons

120
Q

what is always lost or gained during oxidation and reduction?

A

energy

121
Q

Hydrolysis reactions

A
  • addition of water molecule ito 2
  • catabolic process(breaking down)
  • releases energy
122
Q

condensation reactions(dehydration synthesis)

A
  • removal of water molecules to bind 2 molecules together
  • anabolic process(build)
  • absorbs energy
123
Q

when was the fluid mosiac model developed?

A

1972

124
Q

what is the cell membrane made of

A

phospholipid bilayer

125
Q

what is the cell membrane polar end attracted to

A

water

126
Q

what happens to the nonpolar ends of the cell membrane

A

they are repelled

127
Q

what is embedded in the cell membrane

A

protein

128
Q

what do proteins serve in the cell membrane

A

can serve in communication, transport, or strcutral support

129
Q

proteins and phospholipids can what?

A

float and move past each other

130
Q

wheres the cytoskeleton

A

below the surface of the cell membrane and anchors part of the membrane

131
Q

what does the membrane also contain

A

cholesterol

132
Q

what does cholesterol in the cell membrane allow it do

A

allows it to function at a range of temperatures

133
Q

as temperature increases in the membrane…

A

cholesterol maintains rigidity

134
Q

as temperature decreases in the membrane…

A

cholesterol keeps the cell fluid

135
Q

what type of permeable type is the membrane

A

selective permeable

136
Q

what does selective permeable mean

A

allows only specific molecules to pass across

137
Q

name 3 permeable characteristics

A
  1. small non-polar molecules
  2. small polar molecules(water)
  3. large nonpolar (hydrocarbon)
138
Q

name 3 nonpermeable characteristics

A
  1. large polar molecules(sucrose, nucleic acids)
  2. ions(sodium, potassium)
  3. large charged molecules(proteins)
139
Q

what is a special case in the permeable vs nonpermeable

A

WATER

140
Q

Brownian motion

A

the randomness movement of particles

141
Q

particle theory

A
  1. all matter is made up of particles
  2. there are spaces between these particles
  3. the particles are always moving(vibrating)
142
Q

what’s passive transport

A

the movement of molecules across a semipermeable membrane that does not require the cell to expand any energy

143
Q

state the types of passive transport:

A

diffusion, osmosis, facilitated diffusion

144
Q

diffusion?

A

the movement of particles down a concentration gradient from an area of high concentration to an area of low concetration

145
Q

what causes diffusion

A

molecular collisions

146
Q

what will have more collisions? areas of high or areas of low concentration

A

areas of high

147
Q

diffusion rates are effected by what?

A

temperature and pressure

148
Q

what’s free to diffuse across a cell membrane

A

oxygen and carbon dioxide

149
Q

what’s osmosis?

A

the diffusion of water molecules across a selectively permeable membrane from an area of high concetration to an area of low concetration

150
Q

solute

A

substance which dissolve in water
(ex. salt)

151
Q

solvent

A

substances which the solute is dissolve in

152
Q

facilitated diffusion

A

method of diffusion used by molecules that are simply too large to pass through the membrane by diffusion

153
Q

imbedded specialized transport proteins do what in facilliated diffusion

A

move the molecule across

154
Q

transport proteins only do what?

A

only recognize and move one type of dissolved molecule( very selective due to their structure)

155
Q

carrier proteins

A

only accept non charged particles

156
Q

channel proteins

A

will accept charged particles

157
Q

a positively charged channel with only allow what?

A

negatively charged ions to pass and vice versa

158
Q

active transport

A

movement across the cell membrane that REQUIRES the cell to expend energy and moves particles against the concentration gradient

159
Q

how does active transport differ from passive transport

A

does not move with the concentration gradient

160
Q

what does the amount of energy the cell expends on depends on?

A

concentration gradient

161
Q

whats an example of active transport

A
  1. kidney cells need to pump glucose and amino acids into the blood
  2. intestinal cells need to pump nutrients out of the intestine and into the blood
162
Q

sodium-potassium pump

A

protein pumps found in the membrane can move substances against the concentration gradient

163
Q

what do sodium potassium pumps utilize

A

energy from metabolism specifically in the form of ATP

164
Q

where is the sodium potassium pump found in

A

animal cells(every cell in your body)

165
Q

how does the sodium-potassium pump work

A
  1. 3 Na+ ions within the cell bond to the transporter protein at the same time as 2K+ ions bind to the outside of the cell
  2. this causes the protein to change shape
  3. its new shape forces the Na+ ions out and the K+ into the cell
  4. once released, the proteins changes back to its original shape
  5. a high concentration of Na+ builds up outside the cell
  6. Na+ diffuses back inside if it has bonded with a glucose molecule
  7. Na+ returns to the cell down the concentration gradient and this provides the mean for glucose to enter the cell
166
Q

name the two subgroups of bulk active transport

A

endocytosis and exocytosis

167
Q

endocytosis

A

active process by which cells ingest material

168
Q

what’s a vesicle

A

membrane enclosed sac

169
Q

name the two types of endocytosis

A

1.Phagocytosis
2. Pinocytosis

170
Q

phagocytosis

A

movement of a large molecule into the cell

171
Q

pinocytosis

A

transport of fluid droplets into the cell

172
Q

exocytosis

A

active process by which cells export materials

173
Q

what does exocytosis restore

A

the membrane removed by endocytosis

174
Q

isotonic

A

water concentration inside the cell is equal to the concentration outside the cell

175
Q

net movement of isotonic environments

A

0

176
Q

hypotonic

A

water concentration outside the cell is greater than the water concentration inside the cell

177
Q

net movement of hypotonic environments

A

outside to inside

178
Q

hypertonic

A

water concentration inside the cell is greater than the water concentration outside the cell

179
Q

net movement of hypertonic

A

inside to outside

180
Q

plants in what environment have increased turgor pressure

A

hypotonic and its a sign of a healthy plant

181
Q

what’s also known as plasmolysis

A

plants in a hypertonic environment and they will wilt and the cell membrane shrinks away from the cell wall

182
Q

an enzyme is a what?

A

A protein

183
Q

enzymes acts as what

A

A catalyst

184
Q

catalyst

A

speeds up reactions without being consumed in the process

185
Q

substrate

A

the reactant upon which an enzyme acts on

186
Q

active sites

A

depressions on enzymes

187
Q

induced fit

A

when substrate binds to the active site, the enzyme can make subtle changes in shape to accomodate the substrate

188
Q

an enzyme can speed up a reaction by:

A
  1. causing stress on the bonds of the substrate by bending/stretching existing bonds
  2. transferring H+ and OH- ions to or from the substrate to aid hydrolysis and condensation reactions
  3. can accept electron forming a temporary bond, making the substrate less stable
  4. bring 2 substrates together in the correct orientation for reaction
189
Q

factors affecting enzyme function

A

A) temperature
B) pH
c) concentration

190
Q

as temperature increases

A

the activity of the enzyme also increases up to a certain critical temp beyond beyond which enzyme function is impaired
- too hot -> denatured

191
Q

most human enzymes work best between

A

35-40 degrees celcius(close to human body temp)

192
Q

most enzymes pH

A

usually between 6-8

193
Q

whats an exception for enzyme pH

A

pepsin( the enzyme that digests protein in the stomach) works optimally at a pH of 2

194
Q

increasing substrate concentration

A

increases the rate of reaction . becuase more substrate molecules will be colliding with enzyme molecules, so more product will be formed

195
Q

increasing enzyme concentration

A

will increase the rate of reaction, as more enzmes will be colliding with substrate molecules

196
Q

rate of reaction __ as substrate is used up

A

decreases

197
Q

3 types of regulations of enzyme activity

A

A) inhibitors
B) activators
C) cofactors/ coenzymes

198
Q

inhibitors

A
  • shut down the action of the enzyme
199
Q

2 types of inhibitors

A

i) non-competitive inhibitors
ii) competitive inhibitors

200
Q

non-competiitve inhibitors

A

binds to locations other than the active site, called ALLOSTERIC SITES, thus preventing the substrate from binding to the active site by causing a conformation change that alters the active site so that its no longer an ideal receptacle for the substrate.

201
Q

competitive inhibitors

A

bind directly to part of or entire active site by mimicking the shape of the substrate thus preventing the enzyme from accepting the substrate.

202
Q

activators

A

bind to allosteric sites enhancing the activity of the activity of the enzyme by conforming the shape of the enzyme so that the receptacle is a better fit for the substrate

203
Q

cofactors/ coenzymes

A

located in the active site of the enzymes, they attract electrons from the substrate molecule bonds causing them to break

204
Q

cofactors

A

inorganic ions such as copper, zinc and iron

205
Q

Coenzymes

A

Organic, nonproteins molecules

bio12 (3 decks)

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