Unit 1 Flashcards
1
Q
Define Atom
A
Smallest stable unit of matter that has the characteristics of its specific element
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)
3
Q
Protons have a ____ charge
A
Positive
4
Q
Neutrons have ____ charge
A
No
(They are neutral)
5
Q
Electrons have a _____ charge
A
Negative
6
Q
If the orbital is closer to the nucleus, it is a ____ level orbital
A
Low
7
Q
If the orbital is farther to the nucleus, it is a ____ level orbital
A
High
8
Q
What is a valence electron
A
Electron found in the outer most orbital used for making different types of bonds
9
Q
Most elements want ____ electrons in their valence shell because this makes them the ____
A
8
Most stable
10
Q
What’s another way to say non-neutral atom? (Not same number of electrons and protons)
A
Ions
11
Q
What is a cation?
A
An ion with a positive charge because there are more protons than electrons
12
Q
What is an anion
A
An ion with a negative charge because there are more electrons than protons
13
Q
What are the main elements of life
A
Carbon, Hydrogen, oxygen, nitrogen
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.
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.
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.
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.
18
Q
True or False: Organisms in carbon-depleted areas can survive.
A
False
They cannot make the necessary biological molecules without sufficient carbon.
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.
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.
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.
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.
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.
24
Q
Fill in the blank: Nitrogen is recycled into the environment by _______.
A
decomposers
25
True or False: All organisms can synthesize proteins and nucleic acids without nitrogen.
False
## Footnote
Nitrogen is a critical component of proteins and nucleic acids.
26
What is phosphorus used to build?
Nucleic acids and certain types of lipids (phospholipids)
## Footnote
Phosphorus is essential for the structural integrity of nucleic acids and the formation of phospholipids, which are crucial for cell membranes.
27
What happens to organisms in phosphorus depleted areas?
They will die because they cannot make nucleic acids or phospholipids
## Footnote
Nucleic acids are vital for genetic information, while phospholipids are major components of cell membranes.
28
Fill in the blank: Phosphorus is essential for the formation of _______.
Nucleic acids and phospholipids
29
True or False: Phosphorus is not necessary for cell membrane structure.
False
## Footnote
Phosphorus is a key component of phospholipids, which are essential for cell membrane structure.
30
What is electronegativity?
Electronegativity is the measurement of how strongly atoms attract bonding electrons to themselves.
## Footnote
It quantifies the tendency of an atom to attract electrons in a chemical bond.
31
What does electronegativity measure?
Electronegativity measures how much atoms will pull electrons toward themselves.
## Footnote
This is important in understanding bond characteristics and molecular polarity.
32
What determines electronegativity?
Electronegativity is determined by how many electrons are in the valence shell.
## Footnote
Valence electrons play a crucial role in chemical bonding and reactivity.
33
How does the number of valence electrons affect electronegativity?
The closer to eight electrons an element has, the more electronegative it is.
## Footnote
This is based on the octet rule, which states that atoms are more stable with a full valence shell.
34
List 3 electronegative elements you need to know in order of most to least electronegative
Fluorine (most electronegative element)
Oxygen
Nitrogen
35
What is electropositivity?
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
36
Define covalent bonding
37
Define ionic bonding
38
What are polar molecules?
Molecules that occur when there is unequal sharing of electrons across a covalent bond.
## Footnote
Polar molecules have distinct positive and negative ends due to the difference in electronegativity between the atoms involved.
39
What causes the formation of polar molecules?
The bonding of a very electronegative element to a very small or very electropositive element.
## Footnote
This unequal sharing leads to partial charges within the molecule.
40
Polar molecules have an overall ____ charge BUT have a ____ and a ____ charge on its poles
Neutral charge
Partial positive
partial negative
41
Electro negative element will be partially ____ because it’s pulling _____ toward itself
Negative
Electrons
42
Electro positive element will be partially ____ because has ____ electron density near itself
Positive
Less
43
What are hydrogen bonds
Weak attraction between a hydrogen bonded to and oxygen, nitrogen, or fluorine or another O N or F atom
44
Why do hydrogen bonds use only O N and F
45
How atoms are bonded together determine their ____.
Shape
46
The ___ ____ and ____ of a molecule determine its function
Structure, shape, chemical properties
47
What is the law of conservation
48
How does water help maintain homeostasis?
It allows for the transport of materials in different organisms
49
What type of molecule is water?
Water is a polar molecule
## Footnote
A polar molecule has a partial positive charge on one end and a partial negative charge on the other.
50
What do the partial charges on the poles of water molecules do?
Attract to opposite charges on other molecules nearby
## Footnote
This interaction is crucial for various biological and chemical processes.
51
What allows water to hydrogen bond with other water, polar or charged molecules?
Water's polarity
## Footnote
Hydrogen bonding is essential for many properties of water and biological interactions.
52
What are some chemical properties of water due to its polarity?
* Exhibit cohesion and adhesion
* Have surface tension
* Resist temperature changes
* Act as an excellent solvent
## Footnote
These properties play a significant role in supporting life and influencing environmental processes.
53
Define cohesion and adhesion
Co- when water molecules stick to each other
Ad- the tendency of water molecules to stick to materials other than water
54
What cause surface tension in water
The fact water is cohesive
55
What does water exhibit because it is capable of both cohesion and adhesion
Capillary action
56
How does surface tension work?
57
What is capillary action
58
What are hydrogen bonds described as?
Individually weak but collectively strong
## Footnote
Hydrogen bonds play a crucial role in the properties of water and biological molecules.
59
What characteristic of liquid water is attributed to hydrogen bonds?
Constantly breaking and reforming
## Footnote
This dynamic nature of hydrogen bonds contributes to the unique properties of water.
60
What takes a lot of energy to break in water?
All of the hydrogen bonds
## Footnote
Breaking all hydrogen bonds is necessary for water to transition from liquid to gas.
61
What phenomenon does the strong hydrogen bonding in water contribute to?
Resistance to temperature change
## Footnote
This property is essential for various ecological and physiological processes.
62
What is the term for water's ability to resist temperature change?
High Specific Heat Capacity
## Footnote
This property allows water to stabilize temperatures in environments.
63
Why is high specific heat capacity useful for living organisms?
It helps maintain a constant internal temperature for homeostasis
## Footnote
Homeostasis is critical for the survival of organisms.
64
What is a solvent?
Substance that dissolves other chemicals.
65
Why is water considered an excellent solvent?
Because it is polar.
66
What does water do to ionic compounds like salt?
Pulls them apart into ions.
67
What are ions referred to in the context of water?
Electrolytes.
68
Why are electrolytes required?
Required for life.
69
What can water create around polar molecules that cannot ionize? Why can they do this?
A water shell.
Molecules that cannot ionize are held by covalent bonds
70
Give an example of a polar molecule that cannot ionize.
Sugar.
71
What is the role of sugar in biological processes?
Used for cellular respiration.
72
What is the density relationship between solid water and liquid water?
Solid water is less dense than liquid water.
73
What happens to hydrogen bonds as water freezes?
The hydrogen bonds become rigid and stop moving.
74
What effect does freezing have on water molecules regarding its size?
Freezing pushes the water molecules around, expanding the liquid.
75
Fill in the blank: As water freezes, the hydrogen bonds become _______.
rigid
76
What is a biomolecule
Organic carbon based macromolecules
77
True or false: all living organisms need biomolecules
True
78
Why are all life forms carbon based?
79
What’s a monomer, dimer, and polymer
Individual subunit (building block of a macromolecule)
Two monomers covalently bonded together
Many monomers covalently bonded together
80
What is Catabolism, what type of reaction is it?
A type of metabolism
81
What is anabolism, what type of reaction is it?
A type of metabolism (ANBENDERDEHY)
82
What is the relationship between exergonic and endergonic reactions called, and why are they called this?
83
What is dehydration synthesis?
Process by which monomers are covalently bonded together into polymers
## Footnote
Dehydration synthesis is crucial for forming complex molecules from simpler ones.
84
Is dehydration synthesis an anabolic or catabolic process?
Anabolic
(ANBENDERDEHY)
## Footnote
Anabolic processes build larger molecules from smaller ones, utilizing energy.
85
What is the role of enzymes in dehydration synthesis?
Assistance in the process
## Footnote
Enzymes speed up the reactions involved in dehydration synthesis.
86
What does dehydration refer to in dehydration synthesis?
Removal of water
## Footnote
This removal is essential for forming bonds between monomers.
87
What does synthesis mean in the context of dehydration synthesis?
To make (a bond)
## Footnote
Synthesis indicates the creation of new chemical bonds.
88
What is formed as a byproduct of dehydration synthesis?
Water
## Footnote
The creation of polymers involves the release of water molecules.
89
Fill in the blank: Dehydration synthesis is the removal of water to make a bond between _______.
monomers
## Footnote
Monomers are the basic building blocks that combine to form polymers.
90
What is hydrolysis?
Process by which polymers are broken down into monomers
## Footnote
Hydrolysis is essential for the digestion of complex molecules.
91
Is hydrolysis a catabolic or anabolic process?
Catabolic process
(EXERHYDROCAT)
## Footnote
Catabolic processes involve the breakdown of larger molecules into smaller ones.
92
What is required for hydrolysis to occur?
Assistance of enzymes and the breakdown of water
## Footnote
Enzymes facilitate the chemical reactions needed for hydrolysis.
93
What do the terms 'Hydro' and 'Lysis' mean in hydrolysis?
'Hydro' means water and 'Lysis' means to break (a bond)
## Footnote
This reflects the mechanism of hydrolysis where water is used to break chemical bonds.
94
How does hydrolysis utilize water?
Uses water to break the bond between monomers
## Footnote
This process is crucial for converting complex carbohydrates, proteins, and fats into their respective building blocks.
95
What are carbohydrates commonly referred to as?
Sugars
## Footnote
Carbohydrates are a major class of biomolecules that include sugars.
96
What are the monomers of carbohydrates called?
Monosaccharides
## Footnote
Simple sugars like glucose are examples of monosaccharides.
97
What are the polymers of carbohydrates known as?
Polysaccharides
## Footnote
Complex carbohydrates include starches and cellulose.
98
What is the structure of polysaccharides typically characterized by?
Hexamer Rings
## Footnote
This refers to the ring structure often found in polysaccharides like amylose.
99
What is one of the main functions of carbohydrates?
Short term energy source
## Footnote
Carbohydrates provide immediate energy for cellular processes.
100
Name a function of carbohydrates.
Energy storage
## Footnote
Carbohydrates serve as a reserve of energy in organisms.
101
What structural role do carbohydrates play in plants?
Cellulose
## Footnote
Cellulose provides structural integrity to plant cell walls.
102
What structural component do carbohydrates provide in insects and crabs?
Chitin
## Footnote
Chitin serves as a key structural element in the exoskeletons of these organisms.
103
What is the elemental composition of carbohydrates and its ratio
Carbon, hydrogen, oxygen at a ratio of 1C 2H 1O
104
What is glucose?
A monosaccharide that is broken down during aerobic cellular respiration to help make ATP energy.
## Footnote
Glucose is a primary source of energy for cells.
105
What role do carbohydrates play in cell membranes?
Help cell types recognize each other.
## Footnote
Carbohydrates on cell membranes can act as recognition sites for other cells.
106
What is the chemical formula for a monosaccharide?
C_6 H_12 O_6
107
How many saccharides are in oligosaccharides
What are 2 examples of oligosaccharides
3-10
Glycoproteins and glycolipids
108
What’s a glycosidic bond
Bonds formed when two glucose modules undergo dehydration synthesis
109
What is the structure of energy storing carbohydrates. Why are they like this?
110
What is the structure of structural carbohydrates. Why are they like this?
111
Why can’t humans digest cellulose?
It’s made of beta glucose molecules humans dint have the enzyme to digest the beta glucose glycosisdic bonds
112
What is amylose and cellulose
113
Lipids are commonly referred to as _______ or oils.
fats
## Footnote
Lipids include a variety of compounds that are hydrophobic.
114
What are the monomers of lipids?
fatty acids
## Footnote
Fatty acids are the building blocks of lipids.
115
What are the polymers of lipids?
lipids
## Footnote
Lipids are formed from the combination of fatty acids.
116
List the main functions of lipids.
* Long term energy storage
* Insulation
* Protection of organs
## Footnote
These functions are vital for maintaining bodily health.
117
What is the structure of lipids?
Long hydrocarbon chains
## Footnote
The structure contributes to the hydrophobic nature of lipids.
118
What is the elemental composition of lipids?
* Carbon
* Hydrogen
* Oxygen
## Footnote
The ratio is typically 1C: 2H: very little oxygen.
119
What are phospholipids?
120
True or false: lipids are hydrophilic
False they are hydrophobic (avoid water)
121
What are triglycerides made up of?
A glycerol and 3 fatty acids
122
What is a function of a triglycerides
Long term energy storage molecule
123
What’s glycerol
3 carbon compound with 3 -OH groups attached at each carbon
124
What are the structural properties of saturated fats
125
What are the structural properties of unsaturated fats
126
What is the structure of a phospholipid
127
What’s a wax in relation to lipids
128
Steroid is an example of of a ____
Lipid
129
What does a steroid look like?
Four carbon rings bonded together Many monomers
130
Vitamins are ____
Organic compounds essential for efficient, metabolic processes
131
Nucleic acids are commonly referred to as _____
Genetic material
132
The 3 parts of a Nucleotide are ____ and are linked by ___
Sugar, Phosphate, Nitrogenous base
Covalent bonds
133
What are the polymers of nucleotides?
Nucleic acids
134
What’s the elemental composition of a nucleotide
Carbon, Hydrogen, Oxygen, Nitrogen, and Phosphorus
135
What’s the main function nucleus acids
Storage of genetic material
136
What are the two types of nucleic acids
DNA and RNA
137
DNA and RNA have _____ with a ___ end and a ____ end
Directionality
5’
3’
138
What are the similarities and difference between DNA and RNA
139
If one strand of a DNA molecule has the sequence 5’ATTGCA3’ the other complementary strand of the sequence:
5’ TGCAAT 3’
ask someone but I think it’s right
140
All biomolecules are broken down for energy except _____
Nucleic acids
141
142
What are the 4 levels of protein structure?
Primary, Secondary, Tertiary, Quaternary (not all proteins use this)
143
Each level of the protein structure ______ on the others and is held together by _____ bonds and interactions formed between _______
Builds, different, amino acids
144
Proteins are commonly found in _ and __
Meats, muscles
145
The monomers of proteins are ___ and the polymers are ____
Amino acids, polypeptides
146
The elemental structure of proteins is
Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur
147
The main functions of proteins are ___ ___ ___
Wound and tissue repair, catalyzing chemical reactions, cell signaling
148
Enzymes are:
Specialized proteins that catalyze chemical reactions in cells to help maintain homeostasis
149
What is the directionality of proteins?
Proteins have directionality with a distinct N terminus and C terminus
## Footnote
Directionality refers to the orientation of the polypeptide chain, which is crucial for protein function.
150
Where is the N terminus located in a protein chain?
At the first amino acid in the chain
## Footnote
The N terminus has a free amine group.
151
What group is free at the N terminus of a protein?
Amine group
## Footnote
This is the functional group that contributes to the basic properties of amino acids.
152
Where is the C terminus located in a protein chain?
On the last amino acid in the chain
## Footnote
The C terminus has a free carboxyl group.
153
What group is free at the C terminus of a protein?
Carboxyl group
## Footnote
This group is responsible for the acidic properties of amino acids.
154
Image of amino acid structure with info
155
Each amino acid had the same ___
The only difference between each amino acid is ___
“peptide backbone”
The structure and chemical properties of the R side Chain
156
Hydrophobic R groups usually have
Long hydrocarbon chains and big hexamer
157
Hydrophillic R groups usually have
Oxygen or nitrogen in the side chain with no charges
158
Acidic Hydrophillic R groups usually have
Carboxyl groups and negative charges
159
Basic Hydrophillic R groups usually have
Amine groups and positive charges
160
What is the primary protein structure?
The sequence of amino acids formed via protein synthesis.
## Footnote
The primary structure is crucial for the protein's function and stability.
161
What determines how a protein folds at all levels?
The amino acid sequence.
## Footnote
Proper folding is essential for the protein's functionality.
162
What is the consequence of changing the amino acid sequence in a protein?
It usually causes the protein to misfold and stop working.
## Footnote
Misfolded proteins can lead to various diseases.
163
True or False: Misfolded proteins can lead to disease or death.
True.
## Footnote
Protein misfolding is associated with many serious health conditions.
164
What is the primary structure of a protein?
The primary structure is formed when two amino acids are covalently bonded together via dehydration synthesis.
## Footnote
This structure is the first level of protein organization.
165
What type of bond is formed between two amino acids?
Peptide bond
## Footnote
A peptide bond is a covalent bond formed between two amino acids.
166
What process is involved in the formation of a peptide bond?
Dehydration synthesis
## Footnote
This process involves the removal of a water molecule.
167
What role does enzymatic RNA play in the formation of the primary protein structure?
It helps in the formation of peptide bonds in ribosomes.
## Footnote
Enzymatic RNA, or ribozymes, catalyze the reaction.
168
Where does the peptide bond form between amino acids?
Between the carboxyl group of the first amino acid and the amine group of the second.
## Footnote
This specific interaction is crucial for the structure of proteins.
169
Image of formation of primary protein structure forming
170
What is secondary structure in proteins?
Secondary structure occurs as the protein begins to fold
171
Is the protein active during the secondary structure phase?
No, the protein is not active yet
172
What are the two types of secondary structures in proteins?
* Alpha helices
* Beta pleated sheets
173
What type of bonding holds secondary structures together?
Hydrogen bonding between the carboxyl and amine groups on the peptide backbone
174
Do R groups play a role in the formation of secondary structures?
No, R groups are not involved
175
What is tertiary structure in proteins?
Tertiary structure occurs as the protein finishes folding.
176
When are proteins usually functional in terms of structure?
Proteins are usually functional at the tertiary structure.
177
What controls the formation of tertiary structure in proteins?
Interactions between the R side chains on the amino acids.
178
What is the major driving force behind the formation of tertiary structure?
Hydrophobic collapse.
179
What is hydrophobic collapse
180
What type of bond is formed between side chains with electronegative atoms?
Hydrogen bonds
## Footnote
Hydrogen bonds typically involve oxygen (O) and nitrogen (N) atoms.
181
What type of charge attraction occurs between acidic and basic charges?
Charge attraction
## Footnote
Acidic charges are negatively charged (-) and basic charges are positively charged (+).
182
What factors can break hydrogen bonds and charge attractions in proteins?
Changes in pH and temperature
## Footnote
These interactions are sensitive to environmental conditions.
183
True or False: Hydrogen bonds and charge attractions in proteins remain intact outside the normal pH or temperature range.
False
## Footnote
These bonds will be broken if the protein is outside of the normal pH or temperature range.
184
Fill in the blank: Hydrogen bonds and charge attractions are sensitive to changes in _______ and _______.
pH; temperature
## Footnote
These factors can significantly affect protein structure and function.
185
What are disulfide bridges
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
What do more disulfide bridges indicate about a protein's structure?
Stronger structure
## Footnote
Disulfide bridges contribute to the stability of protein structures.
187
Which amino acid is primarily involved in the formation of disulfide bridges?
Cysteine
## Footnote
Cysteine contains a thiol group that can form disulfide bonds.
188
Do cysteine amino acids need to be near each other in the sequence to form disulfide bonds?
No
## Footnote
Cysteine residues can be far apart in the primary structure and still form bonds.
189
In what types of conditions are disulfide bridges usually found in proteins?
Harsh conditions such as
* High temperature
* Extreme pH
## Footnote
These conditions can challenge protein stability, making disulfide bridges important.
190
What is quaternary structure?
Quaternary structure occurs when multiple proteins come together to form a protein complex.
191
What level of folding do proteins in quaternary structure have?
These proteins are all folded at the tertiary level.
192
Are all proteins involved in quaternary structures?
Not all proteins are involved in quaternary structures.
193
What interactions hold quaternary structures together?
Held together by interactions between the variable side chains and hydrogen bonding between the peptide backbones of the different proteins.
194
How do enzymes look in a written chemical reaction?
195
Are Endergonic reactions spontaneous?
Energy is:
DeltaG is___ than zero
No
Absorbed
Greater
196
Are exergonic reactions spontaneous?
Energy is:
DeltaG is___ than zero
Yes
Released
Less than
197
DeltaG/ Free energy is;
Energy that is available to do work in a cell
198
What is a substrate?
Reactant that is changed by the enzyme
199
What is the active site of an enzyme?
Where the substrate binds. It matches the shape of the enzyme and has the correct chemical properties to bind together.
200
What is the enzyme-substrate complex
When the enzyme and substrate are bound together
201
What are enzymes?
Biological catalysts that speed up chemical reactions in the body
202
What is the role of enzymes in the body?
To speed up chemical reactions so they go fast enough to maintain homeostasis
203
Are enzymes used up in chemical reactions?
No, they are reusable and not changed in the reaction
204
What is the relationship between an enzyme's active site and its substrate?
The shape and chemical properties of an enzyme active site are complementary to the shape of the substrate
205
True or False: Enzymes are specific to their substrate.
True
206
What are enzymes primarily made of?
Protein
207
What is the induced fit model of enzyme binding?
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
All chemical reactions require a certain amount of energy. What’s this energy called?
Activation energy
209
Enzymes lower the ___ required for the reaction which makes the reaction go _____
Activation energy
Faster
210
How do enzymes affect the energy of a reaction?
It doesn’t add or take away energy from the reaction
211
Pepsin is a enzyme located in the ___ to break down ____ into monomers
Stomach
Proteins
212
Amylase is a enzyme located in the ___ to break down ____into monomers
Mouth
Starches
213
Enzymes in intestines use ____ to break food into nutrients
Hydrolysis
214
What must enzymes be in to work at their most efficient?
Optimal conditions
## Footnote
Optimal conditions vary based on the specific enzyme and its environment.
215
What happens to enzymes outside their optimal conditions?
They will be less efficient and have a lower reaction rate
## Footnote
Efficiency decreases as conditions deviate from the optimum.
216
What occurs to enzymes in extreme conditions?
They will denature
## Footnote
Denaturation eliminates the enzyme's ability to catalyze reactions.
217
What do optimal conditions for enzymes depend on?
The living conditions of the organisms and where they are in the body
## Footnote
Different environments can lead to variations in optimal conditions for enzymes.
218
What is the maximum rate at which enzymes can catalyze reactions?
Different for each Enzyme.
219
What is enzyme efficiency a measure of?
How close to the maximum rate they are working.
220
Name all factors that can affect enzyme rate and efficiency.
* Optimal temperature and pH
* Substrate Concentration
* Enzyme Concentration
* Product Concentration
* Presence of inhibitors
221
Fill in the blank: Enzyme efficiency is a measure of how close to the _______ they are working.
[maximum rate]
222
True or False: Enzyme efficiency is the same for all enzymes.
False.
223
What is one effect of optimal temperature on enzymes?
It can affect enzyme rate and efficiency.
224
What effect does temperature have on enzymes?
Temperature affects the reaction rate of enzymes, with optimal temperatures increasing activity.
225
What happens to enzymes at suboptimal temperatures?
Lack of energy decreases the amount of collisions between the enzyme and substrate, slowing or stopping the reaction rate.
226
What occurs when an enzyme is heated back up to optimal temperature?
The reaction rate increases up to the optimal rate.
227
Fill in the blank: Lack of energy decreases the amount of _______ between the enzyme and substrate.
collisions
228
True or False: Heating an enzyme beyond optimal temperature will continue to increase the reaction rate.
False
229
How does increasing temperature affect enzyme-substrate collisions?
It increases the speed of enzyme-substrate collisions, thus increasing the reaction rate.
230
What happens to enzyme reaction rates at temperatures above optimal levels?
Reaction rate falls to zero
## Footnote
This occurs because denatured enzymes cannot interact with substrates due to improper active site shape.
231
What causes denaturation of enzymes at high temperatures?
Extra energy causes amino acid side chains to move faster, disrupting weak interactions
## Footnote
This disruption affects the secondary and tertiary structure of the enzyme.
232
What is the result of denaturation on enzyme structure?
Disruption of secondary and tertiary structure
## Footnote
Denaturation leads to loss of proper active site shape.
233
How does denaturation affect the active site of an enzyme?
Denatured enzymes do not have proper active site shape
## Footnote
This prevents interaction with substrates.
234
Fill in the blank: Too much energy available at high temperatures causes _______ of enzymes.
[denaturation]
235
What happens when the pH is raised?
It becomes more basic, leading to a high concentration of OH- ions
## Footnote
OH- ions break hydrogen bonds and ionic interactions, causing denaturation of the enzyme.
236
What effect do OH- ions have on enzymes?
They break hydrogen bonds and ionic interactions, disrupting secondary and tertiary structure and causing denaturation
## Footnote
Denaturation results in loss of enzyme functionality.
237
What is the result of lowering the pH?
It becomes more acidic, leading to a high concentration of H+ ions
## Footnote
H+ ions also break hydrogen bonds and ionic interactions, causing denaturation of the enzyme.
238
What do H+ ions do to enzymes?
They break hydrogen bonds and ionic interactions, disrupting secondary and tertiary structure and causing denaturation
## Footnote
This denaturation affects the enzyme's functionality.
239
Fill in the blank: Substances with basic pH's have a high concentration of _______ ions.
OH-
240
Fill in the blank: Substances with acidic pH's have a high concentration of _______ ions.
H+
241
Denatured enzymes do not have the______. This prevents the ____ from binding and ___ or ___ the reaction rate
correct active site shape
Substrate
Lowers
stops
242
How does changing substrate concentration affect enzyme rate?
It alters the likelihood and speed of enzyme-substrate collisions.
## Footnote
This relationship is crucial for understanding enzyme kinetics.
243
What happens to the reaction rate when substrate concentration decreases?
The reaction rate slows down.
## Footnote
This occurs because fewer substrate molecules are available for the enzyme to bind.
244
What is the effect of increasing substrate concentration on reaction rate?
The reaction rate increases.
## Footnote
This increase continues until the maximum rate is reached.
245
What is the maximum rate for an enzyme?
It is the point at which 100% of the enzyme is occupied by substrate.
## Footnote
Beyond this point, adding more substrate does not increase the reaction rate.
246
What are cofactors?
Non-protein small inorganic compounds & ions bound within enzyme molecule
## Footnote
Cofactors are essential for the activity of many enzymes.
247
What are coenzymes?
Non-protein organic molecules that bind near the active site and assist reactions
## Footnote
Coenzymes often act as carriers for chemical groups or electrons during enzymatic reactions.
248
What is competitive inhibition, what’s its effect on enzyme-substrate complex?
249
What is non-competitive inhibition, what’s its effect on enzyme-substrate complex?
250
Inhibitors can bind ___ or ____. ___ inhibitors permanently deactivate an enzyme
Reversibly
Irreversibly
Irreversible
