Chapters 5, 8 Flashcards
1
Q
Macromolecule:
A
A large molecule formed by the joining of smaller molecules, usually by condensation synthesis
2
Q
4 types of macromolecules
A
Carbs, Lipids, Proteins, Nucleic Acids
3
Q
Polymer
A
Long molecule consisting of many identical or similar building blocks linked by covalent bonds
4
Q
Polymers made of
A
Monomers
5
Q
Differences in macromolecules
A
Differ in monomers but chemical mechanism that cells use to make and break polymers is same
6
Q
How monomers are conmected to make macromolecules
A
Condensation or dehydration reaction
7
Q
Condensation reaction (dehydration)
A
A reaction in which two molecules bond together through the loss of water
8
Q
Hydrolysis
A
Process by which polymers are broken down by the addition of water
9
Q
Carbohydrates and uses
A
A group of compounds that include sugars, which functions in energy storage and are used for building materials
10
Q
Monomers of carbs
A
Sugars
11
Q
Monosaccharide
A
A simple sugar that acts as a monomer for disaccharides and polysaccharides
12
Q
General formula for monosaccharides and ex
A
1:2:1
CH2O
Glucose C6H12O6
13
Q
Characteristics of monosaccharides
A
Multiple hydroxyl groups (-OH) and a carbon double bonded to an oxygen
14
Q
In aqueous solutions most sugars form
A
Rings
15
Q
Dissaccharide
A
Two monosaccharides joined by a Glycosidic linkage
16
Q
Glycosidic linkage
A
Covalent bond formed between two monosaccharides by dehydration reaction
17
Q
Maltose made of
A
Glucose + Glucose
Ingredient for brewing beer
18
Q
Lactose made of
A
Glucose + Galactose
Present in milk
19
Q
Sucrose made of
A
Glucose + Fructose
Table sugar
20
Q
Polysaccharide
A
Long polymers of monosaccharides joined by a glycosidic linkage
21
Q
Functioms of polysaccharides
A
- store energy
2. Building materials for structural support
22
Q
Ex of polysaccharides
A
Starch
Glycogen
Cellulose
Chitin
23
Q
Starch
A
Polysaccharide in plants used for energy storage- made of glucose monomers
24
Q
Glycogen
A
Polysaccharide in animals used for energy storage- made of glucose monomers
25
Cellulose
Cellulose makes up the cell walls and plants – made of glucose monomers
26
What is most abundant organic molecule
Cellulose
27
Chitin
Makes up the exoskeleton of anthropods and the cell wall of fungi
28
Lipids all are...
Hydrophobic- mostly nonpolar C-H bonds
29
Main funtion of fats
Energy storage
30
Gram of fat stores...
2x as much energy as a g of polysaccharide
31
Types of lipids
Fats, fatty acids, phospolipids, steroids
32
Fats made of
Glycerol and fatty acid
33
How fats are made
When 3 fatty acids bond to glycerol through a dehydration reaction and form an ester linkage
34
Triglyceride
3 fatty acids joined to a glycerol
35
Why do fats seperate from water
Bc water molecules hydrogen bomd to one another and exclude fats
36
Saturated fatty acid
A fatty acid in which all carbons in the hydrocarbon tail are connected by a single bonds
37
Is saturated fat solid or liquid at room temp? Unsaturated?
Solid for saturated
| Liquid (oils) for unsaturated
38
Unsaturated fatty acid
Fatty acids that contain one or more double bonds between the carbons in the hydrocarbon tail
39
Shape of unsaturated fatty acids
Kinked
40
Phospholipids
Similar to fats but there are only two fatty acids linked to the glycerol
41
What is third hydroxyl group of glycerol joined to
Phosphate group
42
Parts of phospholipid
Hydrophilic head amd hydrophobic tail
43
Phospholipids are main component of...
Cell membrane
44
Steroids
Whippets characterized by a carbon skeleton consisting of four rings with functional groups attached
45
Steroid cam be more than 4 rings if functional group attached to original four rings includes other rings
science
46
Uses of proteins
Structural support, storage, transport of other substances, ENZYME ACTIVITY
47
All proteins are.
Long chains (polymers) made from a set of 20 amino acids linked by peptide bonds
48
What are aminoacids linked by
Peptide bonds
49
Polypeptides
Amino acid chains
50
Proteins have different functions because
the lengths of the chains can be different and sequence of amino acids can be different
51
Why do amino acids behave different
Bc each one has a different R group
52
R groups have what charge?
They are polar, nonpolar, electrically charged, or neutral
53
How are amino acids linked
Through dehydration reaction
54
Primary structure
The unique sequence of amino acids in a long chain
55
Peptide bomds
Bomd formed between amino group of one amino acid and the carboxyl group of another
56
A chadgd in just one amino acid in primary structure can affect
Protein's Structure, properties, and ability to function properly
57
Secondary structure
When the primary structure folds due to hydrogen bonding
58
What holds secondary structure together
Hydrogen bomds that form at regular intervals along polypeptide backbone
59
2 types of secondary structure
Alpha helix amd pleated sheet
60
Tertiary structure
Irregular contortions of a protein molecule due to interactions of side chains
61
When does protein become functional
When it reaches the tertiary structure
62
Interactions that contribute to stability of tertiary structure
Hydrophobic interactions, van der waals, hydrogen bonds, ionic bonds, and disulfide bridges
63
Quarternary structure
The association between two or more tertiary structures
64
Denaturation
Occurs when a protein unravels and loses its native conformation
65
When does denaturation occur
Changes in pH, temperature, or salt concentration
66
Nucleic acids
Made up of monomers called nucleotides
67
Parts of a nucleotide
Nitrogen Base
Phosphate group
Pentose sugar (5 carbon sugar)
68
Sugars in dna and rna
Dna- deoxyribose
| Rna- ribose
69
DNA
Deoxyribonucleic acid: info that programs all the cell's activities
70
Dna bases
Adenine thymine guanine cytosine
71
Dna provides
Directions for its own replication and also directs rna synthesis
72
RNA
Ribonucleic acid- controls protein synthesis
73
Bases in rna
Adenine uracil guanine cytosine
74
Nucleotides are joined by
Covalent bonds called phosphodiester linkages
75
Ends of nucleic acids
3' and 5' carbons of the sugar in the nucleotide
76
Double helix
Two polynucleotides that spiral around an imaginary axis
77
Metabolism
All the chemical processes of the cell
78
What helps regulate the rate or speed of metabolic pathways
Enzymes
79
The smaller the organism, what type of metabolic rate
Higher
80
2 types of metabolic pathways
Catabolic and anabolic
81
Catabolic pathways
Breaking xown complex material into simple parts (release energy)
82
Ex catabolic pathways
Cellular respiration
83
Anabolic pathways
Making simple substances into complex materials (consume energy to build polymers from monomers)
84
Ex of anabolic pathways
Photosynthesis
85
Energy
The capacity to do work
86
Kinetic energy
Energy of motion
87
Most random and unusable form of kinetic energy
Heat
88
Potential energy
The energy stored by matter as a result of its location (has a capacity to do work)
89
Chemical energy
Form of potential energy that is stored in molecules
90
Thermodynamics
Study of the energy transformatioms that occur in a collection of matter
91
1st law of thermodynamics
Energy can be transferred and transformed but cannot be created or destroyed
92
Entropy
Measure of disorder, or randomness
93
2nd law of thermodynamics
Every energy transfer increasess the entropy of the universe
94
Why dont living things violate the 2nd law
Bc incressed disorder and entropy are offset by biological processed that maintain or increase order
95
Free energy
•Order within a system is maintained bt constant free energy input into the system • energy input must exceed free energy lost to entropy to maintain order and power cellular processes
96
Loss of order or free energy flow results in
Death
97
Excess acquired free energy v required free energy expenditure results
Energy storage or growth
98
Insufficient acquired free energy v required free energy expenditure results in loss of
Mass and ultimately the death of the organism
99
Spontaneous reaction
Occur naturally w out the input of energy
100
Nonspontaneous reactions
Do not occur naturally and they will only occur when energy is added
101
Gibbs free energy (G)
The portion of a system's energy that can perform work
102
How do organisms use free emergy
To maintain organization, grow and reproduce
103
If (triangleG: gibbs free emergy) is negative
Reaction is spontaneous
104
If gibbs free energy is positive
Reaction is nonspontaneous
105
Exergonic reactions
A spontaneous reaction in which there is a net loss of free energy
106
Ex exergonic reaction
Cellular respiration (spontaneous)
107
Endergonic reactions
A nonspontaneous reaction in which free energy is absorbed from the surroundings
108
Ex endergonic
Photosynthesis- Nonsponaneous
109
When do reactants have more free energy than the products
Exergonic
110
Equilibrium
When gibbs free energy is 0 but mever bc of constant flow of materials in and out of the cell
111
Order is maintained by coupling cellular processes that increase entropy (have neg changed in free energy) w those that decrease entropy (have positive changes in G)
.
112
ATP
Adenosine triphosphate- energy source used to drive most types of cellular work
113
What happens ATP TO ADP
Free energy becomes available for metabolism
114
The breakig of the final phosphate bond produces
Phosphate, ADP, and energy
115
Is ATP hydrolysis exergonic or endergonic
Exergonic
116
How is ATP regenerated
By the addition of a phosphate to ADP
117
Catalyst
Chemical agent that speeds up a reaction w out beig consumed
118
Enzyme
A protein catalyst that chamges the rate of a reaction w out being consumed
119
Activation energy
The energy needed to initially break the bonds of the reactants
120
Reactants absorb energy from their surroundings for their bonds to break and energy is released when new bonds of the products are formed
.
121
Activation energy is often supllied in the form of
Heat
122
How do enzymes speed up a reaction
They lower the activation energy allowing the reaction to begin sooner
123
Do enzymes change the G for a reaction
No only the rate at which a reaction occurs
124
Are enzymes consumed in a reaction
No
125
Substrate
Reactant that the enzyme acts on
126
Each enzyme catalyzes how many reactions and why
One bc each enzyme has unique shape (tertiary) that can only bind to a specific substrate
127
Active site
The region on the enzyme that binds to the substrate
128
Substrate is held into the actuve site by
Hydrogen bonds and ionic bonds
129
Induced fit model
As the substrate enters the active site it induces the enzyme to change shape so that it fits more snug
130
1 enzyme can act on how many substrate molecules per second
1000
131
Doss the structure of enzymes chamge in a reaction
No
132
When is enzyme saturated
When the concentration of substrate is high enough that all the enzyme's active sites are engaged
133
Enzymes have a specific temperature and pH that is optimal and during which they are most active
.
134
Optimal pH for most enzymes in human body
6-8
135
Cofactors
Any nonprotein molecule that is required for the proper functioning of the enzyme
136
More specific name for cofactor and ex
Coenzyme and vitamins
137
Competitive inhibitors
Molecules that resemble the normal substrate and compete to bind to the active site
138
How to overcome competitive inhibitors
Add more substrate
139
Noncompetitive inhibitors
Inhibitors that bind to another part of the enzyme causing the shape to xhange so the substrate cant bind to the active site
140
Ex of inhibitors
Neeve gas
Pesticides
Antibiotics
141
2 ways to turn off and on enzymes
Allosteric regulation and feedback inhibition
142
Allosteric regulation
Binding of a molecule to a protein that affects the function of the protein at a different site
143
2 forms of enzymes
Actuve form and inactive form
144
Allosteric activator
Stabilizes the conformation that has a functional active site
145
Allosteric inhibitor
Stabilizes the inactive form of the enzyme
146
Place where molecules bind during allosteric regulation
Allosteric site
147
Feedback inhibition
When a metabolic pathway produces the end product which inhibits an enzyme within the pathway causing the pathway to shut down
