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AP BIO > Unit 1 > Flashcards

Unit 1 Flashcards

1
Q

Define Atom

A

Smallest stable unit of matter that has the characteristics of its specific element

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2
Q

What is the structure of an atom?

A

A nucleus (Protons and neutrons) in the middle and electrons orbitals (electrons orbiting around it)

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3
Q

Protons have a ____ charge

A

Positive

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4
Q

Neutrons have ____ charge

A

No
(They are neutral)

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5
Q

Electrons have a _____ charge

A

Negative

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6
Q

If the orbital is closer to the nucleus, it is a ____ level orbital

A

Low

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7
Q

If the orbital is farther to the nucleus, it is a ____ level orbital

A

High

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8
Q

What is a valence electron

A

Electron found in the outer most orbital used for making different types of bonds

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9
Q

Most elements want ____ electrons in their valence shell because this makes them the ____

A

8
Most stable

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10
Q

What’s another way to say non-neutral atom? (Not same number of electrons and protons)

A

Ions

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11
Q

What is a cation?

A

An ion with a positive charge because there are more protons than electrons

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12
Q

What is an anion

A

An ion with a negative charge because there are more electrons than protons

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13
Q

What are the main elements of life

A

Carbon, Hydrogen, oxygen, nitrogen

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14
Q

What is fixed from the atmosphere by plants during photosynthesis?

A

Inorganic carbon

This process is essential for the conversion of carbon dioxide into organic compounds.

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15
Q

What is the main source of biomass in ecosystems?

A

Carbohydrates

Carbohydrates are synthesized during photosynthesis and serve as a fundamental energy source.

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16
Q

List the biomolecules that organisms utilize carbon to produce.

A
  • Carbohydrates
  • Proteins
  • Nucleic acids
  • Lipids

These biomolecules are crucial for cellular structure and function.

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17
Q

What happens to carbon when organisms die?

A

Decomposers recycle the carbon back into the environment

This recycling process is vital for maintaining ecosystem balance.

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18
Q

True or False: Organisms in carbon-depleted areas can survive.

A

False

They cannot make the necessary biological molecules without sufficient carbon.

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19
Q

Fill in the blank: Inorganic carbon is incorporated into _______ during photosynthesis.

A

carbohydrates

This incorporation is a key step in the carbon cycle.

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20
Q

What process is used by bacteria and other decomposers to fix inorganic nitrogen from the atmosphere?

A

Nitrogen fixation

This process involves converting atmospheric nitrogen into a form that plants can absorb.

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21
Q

How do plants utilize fixed nitrogen?

A

Plants absorb nitrogen to produce proteins and nucleic acids

Proteins and nucleic acids are essential for growth and development.

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22
Q

What role do decomposers play in the nitrogen cycle?

A

Decomposers recycle nitrogen back into the environment

This process is crucial for maintaining nitrogen availability in ecosystems.

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23
Q

What happens to organisms in nitrogen-depleted areas?

A

They will die because they cannot make proteins or nucleic acids

Nitrogen is essential for these fundamental biological molecules.

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24
Q

Fill in the blank: Nitrogen is recycled into the environment by _______.

A

decomposers

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25
Q

True or False: All organisms can synthesize proteins and nucleic acids without nitrogen.

A

False

Nitrogen is a critical component of proteins and nucleic acids.

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26
Q

What is phosphorus used to build?

A

Nucleic acids and certain types of lipids (phospholipids)

Phosphorus is essential for the structural integrity of nucleic acids and the formation of phospholipids, which are crucial for cell membranes.

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27
Q

What happens to organisms in phosphorus depleted areas?

A

They will die because they cannot make nucleic acids or phospholipids

Nucleic acids are vital for genetic information, while phospholipids are major components of cell membranes.

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28
Q

Fill in the blank: Phosphorus is essential for the formation of _______.

A

Nucleic acids and phospholipids

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29
Q

True or False: Phosphorus is not necessary for cell membrane structure.

A

False

Phosphorus is a key component of phospholipids, which are essential for cell membrane structure.

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30
Q

What is electronegativity?

A

Electronegativity is the measurement of how strongly atoms attract bonding electrons to themselves.

It quantifies the tendency of an atom to attract electrons in a chemical bond.

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31
Q

What does electronegativity measure?

A

Electronegativity measures how much atoms will pull electrons toward themselves.

This is important in understanding bond characteristics and molecular polarity.

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32
Q

What determines electronegativity?

A

Electronegativity is determined by how many electrons are in the valence shell.

Valence electrons play a crucial role in chemical bonding and reactivity.

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33
Q

How does the number of valence electrons affect electronegativity?

A

The closer to eight electrons an element has, the more electronegative it is.

This is based on the octet rule, which states that atoms are more stable with a full valence shell.

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34
Q

List 3 electronegative elements you need to know in order of most to least electronegative

A

Fluorine (most electronegative element)
Oxygen
Nitrogen

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35
Q

What is electropositivity?

A

A measurement of the ability of elements to donate electrons and form positive ions
They usually have one or two electrons in their valence shells, and they are not very electronegative

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36
Q

Define covalent bonding

A
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37
Q

Define ionic bonding

A
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38
Q

What are polar molecules?

A

Molecules that occur when there is unequal sharing of electrons across a covalent bond.

Polar molecules have distinct positive and negative ends due to the difference in electronegativity between the atoms involved.

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39
Q

What causes the formation of polar molecules?

A

The bonding of a very electronegative element to a very small or very electropositive element.

This unequal sharing leads to partial charges within the molecule.

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40
Q

Polar molecules have an overall ____ charge BUT have a ____ and a ____ charge on its poles

A

Neutral charge
Partial positive
partial negative

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41
Q

Electro negative element will be partially ____ because it’s pulling _____ toward itself

A

Negative
Electrons

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42
Q

Electro positive element will be partially ____ because has ____ electron density near itself

A

Positive
Less

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43
Q

What are hydrogen bonds

A

Weak attraction between a hydrogen bonded to and oxygen, nitrogen, or fluorine or another O N or F atom

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44
Q

Why do hydrogen bonds use only O N and F

A
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45
Q

How atoms are bonded together determine their ____.

A

Shape

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46
Q

The ___ ____ and ____ of a molecule determine its function

A

Structure, shape, chemical properties

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47
Q

What is the law of conservation

A
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48
Q

How does water help maintain homeostasis?

A

It allows for the transport of materials in different organisms

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49
Q

What type of molecule is water?

A

Water is a polar molecule

A polar molecule has a partial positive charge on one end and a partial negative charge on the other.

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50
Q

What do the partial charges on the poles of water molecules do?

A

Attract to opposite charges on other molecules nearby

This interaction is crucial for various biological and chemical processes.

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51
Q

What allows water to hydrogen bond with other water, polar or charged molecules?

A

Water’s polarity

Hydrogen bonding is essential for many properties of water and biological interactions.

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52
Q

What are some chemical properties of water due to its polarity?

A
  • Exhibit cohesion and adhesion
  • Have surface tension
  • Resist temperature changes
  • Act as an excellent solvent

These properties play a significant role in supporting life and influencing environmental processes.

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53
Q

Define cohesion and adhesion

A

Co- when water molecules stick to each other
Ad- the tendency of water molecules to stick to materials other than water

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54
Q

What cause surface tension in water

A

The fact water is cohesive

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55
Q

What does water exhibit because it is capable of both cohesion and adhesion

A

Capillary action

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56
Q

How does surface tension work?

A
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57
Q

What is capillary action

A
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58
Q

What are hydrogen bonds described as?

A

Individually weak but collectively strong

Hydrogen bonds play a crucial role in the properties of water and biological molecules.

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59
Q

What characteristic of liquid water is attributed to hydrogen bonds?

A

Constantly breaking and reforming

This dynamic nature of hydrogen bonds contributes to the unique properties of water.

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60
Q

What takes a lot of energy to break in water?

A

All of the hydrogen bonds

Breaking all hydrogen bonds is necessary for water to transition from liquid to gas.

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61
Q

What phenomenon does the strong hydrogen bonding in water contribute to?

A

Resistance to temperature change

This property is essential for various ecological and physiological processes.

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62
Q

What is the term for water’s ability to resist temperature change?

A

High Specific Heat Capacity

This property allows water to stabilize temperatures in environments.

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63
Q

Why is high specific heat capacity useful for living organisms?

A

It helps maintain a constant internal temperature for homeostasis

Homeostasis is critical for the survival of organisms.

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64
Q

What is a solvent?

A

Substance that dissolves other chemicals.

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65
Q

Why is water considered an excellent solvent?

A

Because it is polar.

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66
Q

What does water do to ionic compounds like salt?

A

Pulls them apart into ions.

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67
Q

What are ions referred to in the context of water?

A

Electrolytes.

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68
Q

Why are electrolytes required?

A

Required for life.

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69
Q

What can water create around polar molecules that cannot ionize? Why can they do this?

A

A water shell.
Molecules that cannot ionize are held by covalent bonds

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70
Q

Give an example of a polar molecule that cannot ionize.

A

Sugar.

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71
Q

What is the role of sugar in biological processes?

A

Used for cellular respiration.

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72
Q

What is the density relationship between solid water and liquid water?

A

Solid water is less dense than liquid water.

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73
Q

What happens to hydrogen bonds as water freezes?

A

The hydrogen bonds become rigid and stop moving.

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74
Q

What effect does freezing have on water molecules regarding its size?

A

Freezing pushes the water molecules around, expanding the liquid.

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75
Q

Fill in the blank: As water freezes, the hydrogen bonds become _______.

A

rigid

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76
Q

What is a biomolecule

A

Organic carbon based macromolecules

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77
Q

True or false: all living organisms need biomolecules

A

True

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78
Q

Why are all life forms carbon based?

A
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79
Q

What’s a monomer, dimer, and polymer

A

Individual subunit (building block of a macromolecule)
Two monomers covalently bonded together
Many monomers covalently bonded together

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80
Q

What is Catabolism, what type of reaction is it?

A

A type of metabolism

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81
Q

What is anabolism, what type of reaction is it?

A

A type of metabolism (ANBENDERDEHY)

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82
Q

What is the relationship between exergonic and endergonic reactions called, and why are they called this?

A
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83
Q

What is dehydration synthesis?

A

Process by which monomers are covalently bonded together into polymers

Dehydration synthesis is crucial for forming complex molecules from simpler ones.

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84
Q

Is dehydration synthesis an anabolic or catabolic process?

A

Anabolic
(ANBENDERDEHY)
## Footnote

Anabolic processes build larger molecules from smaller ones, utilizing energy.

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85
Q

What is the role of enzymes in dehydration synthesis?

A

Assistance in the process

Enzymes speed up the reactions involved in dehydration synthesis.

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86
Q

What does dehydration refer to in dehydration synthesis?

A

Removal of water

This removal is essential for forming bonds between monomers.

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87
Q

What does synthesis mean in the context of dehydration synthesis?

A

To make (a bond)

Synthesis indicates the creation of new chemical bonds.

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88
Q

What is formed as a byproduct of dehydration synthesis?

A

Water

The creation of polymers involves the release of water molecules.

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89
Q

Fill in the blank: Dehydration synthesis is the removal of water to make a bond between _______.

A

monomers

Monomers are the basic building blocks that combine to form polymers.

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90
Q

What is hydrolysis?

A

Process by which polymers are broken down into monomers

Hydrolysis is essential for the digestion of complex molecules.

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91
Q

Is hydrolysis a catabolic or anabolic process?

A

Catabolic process
(EXERHYDROCAT)
## Footnote

Catabolic processes involve the breakdown of larger molecules into smaller ones.

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92
Q

What is required for hydrolysis to occur?

A

Assistance of enzymes and the breakdown of water

Enzymes facilitate the chemical reactions needed for hydrolysis.

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93
Q

What do the terms ‘Hydro’ and ‘Lysis’ mean in hydrolysis?

A

‘Hydro’ means water and ‘Lysis’ means to break (a bond)

This reflects the mechanism of hydrolysis where water is used to break chemical bonds.

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94
Q

How does hydrolysis utilize water?

A

Uses water to break the bond between monomers

This process is crucial for converting complex carbohydrates, proteins, and fats into their respective building blocks.

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95
Q

What are carbohydrates commonly referred to as?

A

Sugars

Carbohydrates are a major class of biomolecules that include sugars.

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96
Q

What are the monomers of carbohydrates called?

A

Monosaccharides

Simple sugars like glucose are examples of monosaccharides.

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97
Q

What are the polymers of carbohydrates known as?

A

Polysaccharides

Complex carbohydrates include starches and cellulose.

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98
Q

What is the structure of polysaccharides typically characterized by?

A

Hexamer Rings

This refers to the ring structure often found in polysaccharides like amylose.

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99
Q

What is one of the main functions of carbohydrates?

A

Short term energy source

Carbohydrates provide immediate energy for cellular processes.

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100
Q

Name a function of carbohydrates.

A

Energy storage

Carbohydrates serve as a reserve of energy in organisms.

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101
Q

What structural role do carbohydrates play in plants?

A

Cellulose

Cellulose provides structural integrity to plant cell walls.

102
Q

What structural component do carbohydrates provide in insects and crabs?

A

Chitin

Chitin serves as a key structural element in the exoskeletons of these organisms.

103
Q

What is the elemental composition of carbohydrates and its ratio

A

Carbon, hydrogen, oxygen at a ratio of 1C 2H 1O

104
Q

What is glucose?

A

A monosaccharide that is broken down during aerobic cellular respiration to help make ATP energy.

Glucose is a primary source of energy for cells.

105
Q

What role do carbohydrates play in cell membranes?

A

Help cell types recognize each other.

Carbohydrates on cell membranes can act as recognition sites for other cells.

106
Q

What is the chemical formula for a monosaccharide?

A

C_6 H_12 O_6

107
Q

How many saccharides are in oligosaccharides
What are 2 examples of oligosaccharides

A

3-10
Glycoproteins and glycolipids

108
Q

What’s a glycosidic bond

A

Bonds formed when two glucose modules undergo dehydration synthesis

109
Q

What is the structure of energy storing carbohydrates. Why are they like this?

A
110
Q

What is the structure of structural carbohydrates. Why are they like this?

A
111
Q

Why can’t humans digest cellulose?

A

It’s made of beta glucose molecules humans dint have the enzyme to digest the beta glucose glycosisdic bonds

112
Q

What is amylose and cellulose

A
113
Q

Lipids are commonly referred to as _______ or oils.

A

fats

Lipids include a variety of compounds that are hydrophobic.

114
Q

What are the monomers of lipids?

A

fatty acids

Fatty acids are the building blocks of lipids.

115
Q

What are the polymers of lipids?

A

lipids

Lipids are formed from the combination of fatty acids.

116
Q

List the main functions of lipids.

A
  • Long term energy storage
  • Insulation
  • Protection of organs

These functions are vital for maintaining bodily health.

117
Q

What is the structure of lipids?

A

Long hydrocarbon chains

The structure contributes to the hydrophobic nature of lipids.

118
Q

What is the elemental composition of lipids?

A
  • Carbon
  • Hydrogen
  • Oxygen

The ratio is typically 1C: 2H: very little oxygen.

119
Q

What are phospholipids?

A
120
Q

True or false: lipids are hydrophilic

A

False they are hydrophobic (avoid water)

121
Q

What are triglycerides made up of?

A

A glycerol and 3 fatty acids

122
Q

What is a function of a triglycerides

A

Long term energy storage molecule

123
Q

What’s glycerol

A

3 carbon compound with 3 -OH groups attached at each carbon

124
Q

What are the structural properties of saturated fats

A
125
Q

What are the structural properties of unsaturated fats

A
126
Q

What is the structure of a phospholipid

A
127
Q

What’s a wax in relation to lipids

A
128
Q

Steroid is an example of of a ____

A

Lipid

129
Q

What does a steroid look like?

A

Four carbon rings bonded together Many monomers

130
Q

Vitamins are ____

A

Organic compounds essential for efficient, metabolic processes

131
Q

Nucleic acids are commonly referred to as _____

A

Genetic material

132
Q

The 3 parts of a Nucleotide are ____ and are linked by ___

A

Sugar, Phosphate, Nitrogenous base

Covalent bonds

133
Q

What are the polymers of nucleotides?

A

Nucleic acids

134
Q

What’s the elemental composition of a nucleotide

A

Carbon, Hydrogen, Oxygen, Nitrogen, and Phosphorus

135
Q

What’s the main function nucleus acids

A

Storage of genetic material

136
Q

What are the two types of nucleic acids

A

DNA and RNA

137
Q

DNA and RNA have _____ with a ___ end and a ____ end

A

Directionality
5’
3’

138
Q

What are the similarities and difference between DNA and RNA

A
139
Q

If one strand of a DNA molecule has the sequence 5’ATTGCA3’ the other complementary strand of the sequence:

A

5’ TGCAAT 3’
ask someone but I think it’s right

140
Q

All biomolecules are broken down for energy except _____

A

Nucleic acids

141
Q
A
142
Q

What are the 4 levels of protein structure?

A

Primary, Secondary, Tertiary, Quaternary (not all proteins use this)

143
Q

Each level of the protein structure ______ on the others and is held together by _____ bonds and interactions formed between _______

A

Builds, different, amino acids

144
Q

Proteins are commonly found in _ and __

A

Meats, muscles

145
Q

The monomers of proteins are ___ and the polymers are ____

A

Amino acids, polypeptides

146
Q

The elemental structure of proteins is

A

Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur

147
Q

The main functions of proteins are ___ ___ ___

A

Wound and tissue repair, catalyzing chemical reactions, cell signaling

148
Q

Enzymes are:

A

Specialized proteins that catalyze chemical reactions in cells to help maintain homeostasis

149
Q

What is the directionality of proteins?

A

Proteins have directionality with a distinct N terminus and C terminus

Directionality refers to the orientation of the polypeptide chain, which is crucial for protein function.

150
Q

Where is the N terminus located in a protein chain?

A

At the first amino acid in the chain

The N terminus has a free amine group.

151
Q

What group is free at the N terminus of a protein?

A

Amine group

This is the functional group that contributes to the basic properties of amino acids.

152
Q

Where is the C terminus located in a protein chain?

A

On the last amino acid in the chain

The C terminus has a free carboxyl group.

153
Q

What group is free at the C terminus of a protein?

A

Carboxyl group

This group is responsible for the acidic properties of amino acids.

154
Q

Image of amino acid structure with info

A
155
Q

Each amino acid had the same ___
The only difference between each amino acid is ___

A

“peptide backbone”
The structure and chemical properties of the R side Chain

156
Q

Hydrophobic R groups usually have

A

Long hydrocarbon chains and big hexamer

157
Q

Hydrophillic R groups usually have

A

Oxygen or nitrogen in the side chain with no charges

158
Q

Acidic Hydrophillic R groups usually have

A

Carboxyl groups and negative charges

159
Q

Basic Hydrophillic R groups usually have

A

Amine groups and positive charges

160
Q

What is the primary protein structure?

A

The sequence of amino acids formed via protein synthesis.

The primary structure is crucial for the protein’s function and stability.

161
Q

What determines how a protein folds at all levels?

A

The amino acid sequence.

Proper folding is essential for the protein’s functionality.

162
Q

What is the consequence of changing the amino acid sequence in a protein?

A

It usually causes the protein to misfold and stop working.

Misfolded proteins can lead to various diseases.

163
Q

True or False: Misfolded proteins can lead to disease or death.

A

True.

Protein misfolding is associated with many serious health conditions.

164
Q

What is the primary structure of a protein?

A

The primary structure is formed when two amino acids are covalently bonded together via dehydration synthesis.

This structure is the first level of protein organization.

165
Q

What type of bond is formed between two amino acids?

A

Peptide bond

A peptide bond is a covalent bond formed between two amino acids.

166
Q

What process is involved in the formation of a peptide bond?

A

Dehydration synthesis

This process involves the removal of a water molecule.

167
Q

What role does enzymatic RNA play in the formation of the primary protein structure?

A

It helps in the formation of peptide bonds in ribosomes.

Enzymatic RNA, or ribozymes, catalyze the reaction.

168
Q

Where does the peptide bond form between amino acids?

A

Between the carboxyl group of the first amino acid and the amine group of the second.

This specific interaction is crucial for the structure of proteins.

169
Q

Image of formation of primary protein structure forming

A
170
Q

What is secondary structure in proteins?

A

Secondary structure occurs as the protein begins to fold

171
Q

Is the protein active during the secondary structure phase?

A

No, the protein is not active yet

172
Q

What are the two types of secondary structures in proteins?

A
  • Alpha helices
  • Beta pleated sheets
173
Q

What type of bonding holds secondary structures together?

A

Hydrogen bonding between the carboxyl and amine groups on the peptide backbone

174
Q

Do R groups play a role in the formation of secondary structures?

A

No, R groups are not involved

175
Q

What is tertiary structure in proteins?

A

Tertiary structure occurs as the protein finishes folding.

176
Q

When are proteins usually functional in terms of structure?

A

Proteins are usually functional at the tertiary structure.

177
Q

What controls the formation of tertiary structure in proteins?

A

Interactions between the R side chains on the amino acids.

178
Q

What is the major driving force behind the formation of tertiary structure?

A

Hydrophobic collapse.

179
Q

What is hydrophobic collapse

A
180
Q

What type of bond is formed between side chains with electronegative atoms?

A

Hydrogen bonds

Hydrogen bonds typically involve oxygen (O) and nitrogen (N) atoms.

181
Q

What type of charge attraction occurs between acidic and basic charges?

A

Charge attraction

Acidic charges are negatively charged (-) and basic charges are positively charged (+).

182
Q

What factors can break hydrogen bonds and charge attractions in proteins?

A

Changes in pH and temperature

These interactions are sensitive to environmental conditions.

183
Q

True or False: Hydrogen bonds and charge attractions in proteins remain intact outside the normal pH or temperature range.

A

False

These bonds will be broken if the protein is outside of the normal pH or temperature range.

184
Q

Fill in the blank: Hydrogen bonds and charge attractions are sensitive to changes in _______ and _______.

A

pH; temperature

These factors can significantly affect protein structure and function.

185
Q

What are disulfide bridges

A

Covalent bonds between the sulfur atoms present in the side chains of two cysteine amino acids. They are very strong and not sensitive to changes in pH or temperature

186
Q

What do more disulfide bridges indicate about a protein’s structure?

A

Stronger structure

Disulfide bridges contribute to the stability of protein structures.

187
Q

Which amino acid is primarily involved in the formation of disulfide bridges?

A

Cysteine

Cysteine contains a thiol group that can form disulfide bonds.

188
Q

Do cysteine amino acids need to be near each other in the sequence to form disulfide bonds?

A

No

Cysteine residues can be far apart in the primary structure and still form bonds.

189
Q

In what types of conditions are disulfide bridges usually found in proteins?

A

Harsh conditions such as
* High temperature
* Extreme pH

These conditions can challenge protein stability, making disulfide bridges important.

190
Q

What is quaternary structure?

A

Quaternary structure occurs when multiple proteins come together to form a protein complex.

191
Q

What level of folding do proteins in quaternary structure have?

A

These proteins are all folded at the tertiary level.

192
Q

Are all proteins involved in quaternary structures?

A

Not all proteins are involved in quaternary structures.

193
Q

What interactions hold quaternary structures together?

A

Held together by interactions between the variable side chains and hydrogen bonding between the peptide backbones of the different proteins.

194
Q

How do enzymes look in a written chemical reaction?

A
195
Q

Are Endergonic reactions spontaneous?
Energy is:
DeltaG is___ than zero

A

No
Absorbed
Greater

196
Q

Are exergonic reactions spontaneous?
Energy is:
DeltaG is___ than zero

A

Yes
Released
Less than

197
Q

DeltaG/ Free energy is;

A

Energy that is available to do work in a cell

198
Q

What is a substrate?

A

Reactant that is changed by the enzyme

199
Q

What is the active site of an enzyme?

A

Where the substrate binds. It matches the shape of the enzyme and has the correct chemical properties to bind together.

200
Q

What is the enzyme-substrate complex

A

When the enzyme and substrate are bound together

201
Q

What are enzymes?

A

Biological catalysts that speed up chemical reactions in the body

202
Q

What is the role of enzymes in the body?

A

To speed up chemical reactions so they go fast enough to maintain homeostasis

203
Q

Are enzymes used up in chemical reactions?

A

No, they are reusable and not changed in the reaction

204
Q

What is the relationship between an enzyme’s active site and its substrate?

A

The shape and chemical properties of an enzyme active site are complementary to the shape of the substrate

205
Q

True or False: Enzymes are specific to their substrate.

A

True

206
Q

What are enzymes primarily made of?

A

Protein

207
Q

What is the induced fit model of enzyme binding?

A

When the substrate binds the enzyme undergoes a conformational change and surrounds the substrate to catalyze the chemical reaction

The enzyme returns to normal once the reaction is complete

208
Q

All chemical reactions require a certain amount of energy. What’s this energy called?

A

Activation energy

209
Q

Enzymes lower the ___ required for the reaction which makes the reaction go _____

A

Activation energy
Faster

210
Q

How do enzymes affect the energy of a reaction?

A

It doesn’t add or take away energy from the reaction

211
Q

Pepsin is a enzyme located in the ___ to break down ____ into monomers

A

Stomach
Proteins

212
Q

Amylase is a enzyme located in the ___ to break down ____into monomers

A

Mouth
Starches

213
Q

Enzymes in intestines use ____ to break food into nutrients

A

Hydrolysis

214
Q

What must enzymes be in to work at their most efficient?

A

Optimal conditions

Optimal conditions vary based on the specific enzyme and its environment.

215
Q

What happens to enzymes outside their optimal conditions?

A

They will be less efficient and have a lower reaction rate

Efficiency decreases as conditions deviate from the optimum.

216
Q

What occurs to enzymes in extreme conditions?

A

They will denature

Denaturation eliminates the enzyme’s ability to catalyze reactions.

217
Q

What do optimal conditions for enzymes depend on?

A

The living conditions of the organisms and where they are in the body

Different environments can lead to variations in optimal conditions for enzymes.

218
Q

What is the maximum rate at which enzymes can catalyze reactions?

A

Different for each Enzyme.

219
Q

What is enzyme efficiency a measure of?

A

How close to the maximum rate they are working.

220
Q

Name all factors that can affect enzyme rate and efficiency.

A
  • Optimal temperature and pH
  • Substrate Concentration
  • Enzyme Concentration
  • Product Concentration
  • Presence of inhibitors
221
Q

Fill in the blank: Enzyme efficiency is a measure of how close to the _______ they are working.

A

[maximum rate]

222
Q

True or False: Enzyme efficiency is the same for all enzymes.

A

False.

223
Q

What is one effect of optimal temperature on enzymes?

A

It can affect enzyme rate and efficiency.

224
Q

What effect does temperature have on enzymes?

A

Temperature affects the reaction rate of enzymes, with optimal temperatures increasing activity.

225
Q

What happens to enzymes at suboptimal temperatures?

A

Lack of energy decreases the amount of collisions between the enzyme and substrate, slowing or stopping the reaction rate.

226
Q

What occurs when an enzyme is heated back up to optimal temperature?

A

The reaction rate increases up to the optimal rate.

227
Q

Fill in the blank: Lack of energy decreases the amount of _______ between the enzyme and substrate.

A

collisions

228
Q

True or False: Heating an enzyme beyond optimal temperature will continue to increase the reaction rate.

A

False

229
Q

How does increasing temperature affect enzyme-substrate collisions?

A

It increases the speed of enzyme-substrate collisions, thus increasing the reaction rate.

230
Q

What happens to enzyme reaction rates at temperatures above optimal levels?

A

Reaction rate falls to zero

This occurs because denatured enzymes cannot interact with substrates due to improper active site shape.

231
Q

What causes denaturation of enzymes at high temperatures?

A

Extra energy causes amino acid side chains to move faster, disrupting weak interactions

This disruption affects the secondary and tertiary structure of the enzyme.

232
Q

What is the result of denaturation on enzyme structure?

A

Disruption of secondary and tertiary structure

Denaturation leads to loss of proper active site shape.

233
Q

How does denaturation affect the active site of an enzyme?

A

Denatured enzymes do not have proper active site shape

This prevents interaction with substrates.

234
Q

Fill in the blank: Too much energy available at high temperatures causes _______ of enzymes.

A

[denaturation]

235
Q

What happens when the pH is raised?

A

It becomes more basic, leading to a high concentration of OH- ions

OH- ions break hydrogen bonds and ionic interactions, causing denaturation of the enzyme.

236
Q

What effect do OH- ions have on enzymes?

A

They break hydrogen bonds and ionic interactions, disrupting secondary and tertiary structure and causing denaturation

Denaturation results in loss of enzyme functionality.

237
Q

What is the result of lowering the pH?

A

It becomes more acidic, leading to a high concentration of H+ ions

H+ ions also break hydrogen bonds and ionic interactions, causing denaturation of the enzyme.

238
Q

What do H+ ions do to enzymes?

A

They break hydrogen bonds and ionic interactions, disrupting secondary and tertiary structure and causing denaturation

This denaturation affects the enzyme’s functionality.

239
Q

Fill in the blank: Substances with basic pH’s have a high concentration of _______ ions.

A

OH-

240
Q

Fill in the blank: Substances with acidic pH’s have a high concentration of _______ ions.

A

H+

241
Q

Denatured enzymes do not have the______. This prevents the ____ from binding and ___ or ___ the reaction rate

A

correct active site shape
Substrate
Lowers
stops

242
Q

How does changing substrate concentration affect enzyme rate?

A

It alters the likelihood and speed of enzyme-substrate collisions.

This relationship is crucial for understanding enzyme kinetics.

243
Q

What happens to the reaction rate when substrate concentration decreases?

A

The reaction rate slows down.

This occurs because fewer substrate molecules are available for the enzyme to bind.

244
Q

What is the effect of increasing substrate concentration on reaction rate?

A

The reaction rate increases.

This increase continues until the maximum rate is reached.

245
Q

What is the maximum rate for an enzyme?

A

It is the point at which 100% of the enzyme is occupied by substrate.

Beyond this point, adding more substrate does not increase the reaction rate.

246
Q

What are cofactors?

A

Non-protein small inorganic compounds & ions bound within enzyme molecule

Cofactors are essential for the activity of many enzymes.

247
Q

What are coenzymes?

A

Non-protein organic molecules that bind near the active site and assist reactions

Coenzymes often act as carriers for chemical groups or electrons during enzymatic reactions.

248
Q

What is competitive inhibition, what’s its effect on enzyme-substrate complex?

A
249
Q

What is non-competitive inhibition, what’s its effect on enzyme-substrate complex?

A
250
Q

Inhibitors can bind ___ or ____. ___ inhibitors permanently deactivate an enzyme

A

Reversibly
Irreversibly
Irreversible

AP BIO (14 decks)

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