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AP Bio T1 > Chapters 5, 8 > Flashcards

Chapters 5, 8 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Macromolecule:

A

A large molecule formed by the joining of smaller molecules, usually by condensation synthesis

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2
Q

4 types of macromolecules

A

Carbs, Lipids, Proteins, Nucleic Acids

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3
Q

Polymer

A

Long molecule consisting of many identical or similar building blocks linked by covalent bonds

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4
Q

Polymers made of

A

Monomers

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5
Q

Differences in macromolecules

A

Differ in monomers but chemical mechanism that cells use to make and break polymers is same

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6
Q

How monomers are conmected to make macromolecules

A

Condensation or dehydration reaction

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7
Q

Condensation reaction (dehydration)

A

A reaction in which two molecules bond together through the loss of water

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8
Q

Hydrolysis

A

Process by which polymers are broken down by the addition of water

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9
Q

Carbohydrates and uses

A

A group of compounds that include sugars, which functions in energy storage and are used for building materials

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10
Q

Monomers of carbs

A

Sugars

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11
Q

Monosaccharide

A

A simple sugar that acts as a monomer for disaccharides and polysaccharides

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12
Q

General formula for monosaccharides and ex

A

1:2:1
CH2O
Glucose C6H12O6

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13
Q

Characteristics of monosaccharides

A

Multiple hydroxyl groups (-OH) and a carbon double bonded to an oxygen

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14
Q

In aqueous solutions most sugars form

A

Rings

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15
Q

Dissaccharide

A

Two monosaccharides joined by a Glycosidic linkage

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16
Q

Glycosidic linkage

A

Covalent bond formed between two monosaccharides by dehydration reaction

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17
Q

Maltose made of

A

Glucose + Glucose

Ingredient for brewing beer

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18
Q

Lactose made of

A

Glucose + Galactose

Present in milk

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19
Q

Sucrose made of

A

Glucose + Fructose

Table sugar

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20
Q

Polysaccharide

A

Long polymers of monosaccharides joined by a glycosidic linkage

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21
Q

Functioms of polysaccharides

A
  1. store energy

2. Building materials for structural support

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22
Q

Ex of polysaccharides

A

Starch
Glycogen
Cellulose
Chitin

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23
Q

Starch

A

Polysaccharide in plants used for energy storage- made of glucose monomers

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24
Q

Glycogen

A

Polysaccharide in animals used for energy storage- made of glucose monomers

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25
Q

Cellulose

A

Cellulose makes up the cell walls and plants – made of glucose monomers

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26
Q

What is most abundant organic molecule

A

Cellulose

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27
Q

Chitin

A

Makes up the exoskeleton of anthropods and the cell wall of fungi

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28
Q

Lipids all are…

A

Hydrophobic- mostly nonpolar C-H bonds

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29
Q

Main funtion of fats

A

Energy storage

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30
Q

Gram of fat stores…

A

2x as much energy as a g of polysaccharide

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31
Q

Types of lipids

A

Fats, fatty acids, phospolipids, steroids

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32
Q

Fats made of

A

Glycerol and fatty acid

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33
Q

How fats are made

A

When 3 fatty acids bond to glycerol through a dehydration reaction and form an ester linkage

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34
Q

Triglyceride

A

3 fatty acids joined to a glycerol

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35
Q

Why do fats seperate from water

A

Bc water molecules hydrogen bomd to one another and exclude fats

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36
Q

Saturated fatty acid

A

A fatty acid in which all carbons in the hydrocarbon tail are connected by a single bonds

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37
Q

Is saturated fat solid or liquid at room temp? Unsaturated?

A

Solid for saturated

Liquid (oils) for unsaturated

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38
Q

Unsaturated fatty acid

A

Fatty acids that contain one or more double bonds between the carbons in the hydrocarbon tail

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39
Q

Shape of unsaturated fatty acids

A

Kinked

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40
Q

Phospholipids

A

Similar to fats but there are only two fatty acids linked to the glycerol

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41
Q

What is third hydroxyl group of glycerol joined to

A

Phosphate group

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42
Q

Parts of phospholipid

A

Hydrophilic head amd hydrophobic tail

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43
Q

Phospholipids are main component of…

A

Cell membrane

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44
Q

Steroids

A

Whippets characterized by a carbon skeleton consisting of four rings with functional groups attached

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45
Q

Steroid cam be more than 4 rings if functional group attached to original four rings includes other rings

A

science

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46
Q

Uses of proteins

A

Structural support, storage, transport of other substances, ENZYME ACTIVITY

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47
Q

All proteins are.

A

Long chains (polymers) made from a set of 20 amino acids linked by peptide bonds

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48
Q

What are aminoacids linked by

A

Peptide bonds

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49
Q

Polypeptides

A

Amino acid chains

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50
Q

Proteins have different functions because

A

the lengths of the chains can be different and sequence of amino acids can be different

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51
Q

Why do amino acids behave different

A

Bc each one has a different R group

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52
Q

R groups have what charge?

A

They are polar, nonpolar, electrically charged, or neutral

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53
Q

How are amino acids linked

A

Through dehydration reaction

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54
Q

Primary structure

A

The unique sequence of amino acids in a long chain

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55
Q

Peptide bomds

A

Bomd formed between amino group of one amino acid and the carboxyl group of another

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56
Q

A chadgd in just one amino acid in primary structure can affect

A

Protein’s Structure, properties, and ability to function properly

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57
Q

Secondary structure

A

When the primary structure folds due to hydrogen bonding

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58
Q

What holds secondary structure together

A

Hydrogen bomds that form at regular intervals along polypeptide backbone

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59
Q

2 types of secondary structure

A

Alpha helix amd pleated sheet

60
Q

Tertiary structure

A

Irregular contortions of a protein molecule due to interactions of side chains

61
Q

When does protein become functional

A

When it reaches the tertiary structure

62
Q

Interactions that contribute to stability of tertiary structure

A

Hydrophobic interactions, van der waals, hydrogen bonds, ionic bonds, and disulfide bridges

63
Q

Quarternary structure

A

The association between two or more tertiary structures

64
Q

Denaturation

A

Occurs when a protein unravels and loses its native conformation

65
Q

When does denaturation occur

A

Changes in pH, temperature, or salt concentration

66
Q

Nucleic acids

A

Made up of monomers called nucleotides

67
Q

Parts of a nucleotide

A

Nitrogen Base
Phosphate group
Pentose sugar (5 carbon sugar)

68
Q

Sugars in dna and rna

A

Dna- deoxyribose

Rna- ribose

69
Q

DNA

A

Deoxyribonucleic acid: info that programs all the cell’s activities

70
Q

Dna bases

A

Adenine thymine guanine cytosine

71
Q

Dna provides

A

Directions for its own replication and also directs rna synthesis

72
Q

RNA

A

Ribonucleic acid- controls protein synthesis

73
Q

Bases in rna

A

Adenine uracil guanine cytosine

74
Q

Nucleotides are joined by

A

Covalent bonds called phosphodiester linkages

75
Q

Ends of nucleic acids

A

3’ and 5’ carbons of the sugar in the nucleotide

76
Q

Double helix

A

Two polynucleotides that spiral around an imaginary axis

77
Q

Metabolism

A

All the chemical processes of the cell

78
Q

What helps regulate the rate or speed of metabolic pathways

A

Enzymes

79
Q

The smaller the organism, what type of metabolic rate

A

Higher

80
Q

2 types of metabolic pathways

A

Catabolic and anabolic

81
Q

Catabolic pathways

A

Breaking xown complex material into simple parts (release energy)

82
Q

Ex catabolic pathways

A

Cellular respiration

83
Q

Anabolic pathways

A

Making simple substances into complex materials (consume energy to build polymers from monomers)

84
Q

Ex of anabolic pathways

A

Photosynthesis

85
Q

Energy

A

The capacity to do work

86
Q

Kinetic energy

A

Energy of motion

87
Q

Most random and unusable form of kinetic energy

A

Heat

88
Q

Potential energy

A

The energy stored by matter as a result of its location (has a capacity to do work)

89
Q

Chemical energy

A

Form of potential energy that is stored in molecules

90
Q

Thermodynamics

A

Study of the energy transformatioms that occur in a collection of matter

91
Q

1st law of thermodynamics

A

Energy can be transferred and transformed but cannot be created or destroyed

92
Q

Entropy

A

Measure of disorder, or randomness

93
Q

2nd law of thermodynamics

A

Every energy transfer increasess the entropy of the universe

94
Q

Why dont living things violate the 2nd law

A

Bc incressed disorder and entropy are offset by biological processed that maintain or increase order

95
Q

Free energy

A

•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
Q

Loss of order or free energy flow results in

A

Death

97
Q

Excess acquired free energy v required free energy expenditure results

A

Energy storage or growth

98
Q

Insufficient acquired free energy v required free energy expenditure results in loss of

A

Mass and ultimately the death of the organism

99
Q

Spontaneous reaction

A

Occur naturally w out the input of energy

100
Q

Nonspontaneous reactions

A

Do not occur naturally and they will only occur when energy is added

101
Q

Gibbs free energy (G)

A

The portion of a system’s energy that can perform work

102
Q

How do organisms use free emergy

A

To maintain organization, grow and reproduce

103
Q

If (triangleG: gibbs free emergy) is negative

A

Reaction is spontaneous

104
Q

If gibbs free energy is positive

A

Reaction is nonspontaneous

105
Q

Exergonic reactions

A

A spontaneous reaction in which there is a net loss of free energy

106
Q

Ex exergonic reaction

A

Cellular respiration (spontaneous)

107
Q

Endergonic reactions

A

A nonspontaneous reaction in which free energy is absorbed from the surroundings

108
Q

Ex endergonic

A

Photosynthesis- Nonsponaneous

109
Q

When do reactants have more free energy than the products

A

Exergonic

110
Q

Equilibrium

A

When gibbs free energy is 0 but mever bc of constant flow of materials in and out of the cell

111
Q

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)

A

.

112
Q

ATP

A

Adenosine triphosphate- energy source used to drive most types of cellular work

113
Q

What happens ATP TO ADP

A

Free energy becomes available for metabolism

114
Q

The breakig of the final phosphate bond produces

A

Phosphate, ADP, and energy

115
Q

Is ATP hydrolysis exergonic or endergonic

A

Exergonic

116
Q

How is ATP regenerated

A

By the addition of a phosphate to ADP

117
Q

Catalyst

A

Chemical agent that speeds up a reaction w out beig consumed

118
Q

Enzyme

A

A protein catalyst that chamges the rate of a reaction w out being consumed

119
Q

Activation energy

A

The energy needed to initially break the bonds of the reactants

120
Q

Reactants absorb energy from their surroundings for their bonds to break and energy is released when new bonds of the products are formed

A

.

121
Q

Activation energy is often supllied in the form of

A

Heat

122
Q

How do enzymes speed up a reaction

A

They lower the activation energy allowing the reaction to begin sooner

123
Q

Do enzymes change the G for a reaction

A

No only the rate at which a reaction occurs

124
Q

Are enzymes consumed in a reaction

A

No

125
Q

Substrate

A

Reactant that the enzyme acts on

126
Q

Each enzyme catalyzes how many reactions and why

A

One bc each enzyme has unique shape (tertiary) that can only bind to a specific substrate

127
Q

Active site

A

The region on the enzyme that binds to the substrate

128
Q

Substrate is held into the actuve site by

A

Hydrogen bonds and ionic bonds

129
Q

Induced fit model

A

As the substrate enters the active site it induces the enzyme to change shape so that it fits more snug

130
Q

1 enzyme can act on how many substrate molecules per second

A

1000

131
Q

Doss the structure of enzymes chamge in a reaction

A

No

132
Q

When is enzyme saturated

A

When the concentration of substrate is high enough that all the enzyme’s active sites are engaged

133
Q

Enzymes have a specific temperature and pH that is optimal and during which they are most active

A

.

134
Q

Optimal pH for most enzymes in human body

A

6-8

135
Q

Cofactors

A

Any nonprotein molecule that is required for the proper functioning of the enzyme

136
Q

More specific name for cofactor and ex

A

Coenzyme and vitamins

137
Q

Competitive inhibitors

A

Molecules that resemble the normal substrate and compete to bind to the active site

138
Q

How to overcome competitive inhibitors

A

Add more substrate

139
Q

Noncompetitive inhibitors

A

Inhibitors that bind to another part of the enzyme causing the shape to xhange so the substrate cant bind to the active site

140
Q

Ex of inhibitors

A

Neeve gas
Pesticides
Antibiotics

141
Q

2 ways to turn off and on enzymes

A

Allosteric regulation and feedback inhibition

142
Q

Allosteric regulation

A

Binding of a molecule to a protein that affects the function of the protein at a different site

143
Q

2 forms of enzymes

A

Actuve form and inactive form

144
Q

Allosteric activator

A

Stabilizes the conformation that has a functional active site

145
Q

Allosteric inhibitor

A

Stabilizes the inactive form of the enzyme

146
Q

Place where molecules bind during allosteric regulation

A

Allosteric site

147
Q

Feedback inhibition

A

When a metabolic pathway produces the end product which inhibits an enzyme within the pathway causing the pathway to shut down

AP Bio T1 (9 decks)

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