Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

AP Biology > Biochemistry > Flashcards

Biochemistry Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

Subatomic Particles in Atoms

A

Protons (+), Neutrons and Electrons (-)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Ground State

A

If all electrons in an atom are in the lowest available energy levels.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Excited State

A

When an atom absorbs, its electrons move to a higher energy level.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Isotopes

A

Atoms of one element that vary only in the number of neutrons in the nucleus. Chemically, all isotopes of the same element are identical because they have the same number of electrons in the same configuration.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Half-Life

A

The rate at which an isotope decays. Enables us to measure the age of fossils or to estimate the age of the Earth.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Tracer

A

Radioisotopes that can be incorporated into a molecule and use to trace the path in a metabolic pathway.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Atom Bonds

A

Atoms bond when two atomic nuclei attract the same electron/s. Energy is released when a bond is formed and energy must be supplies to break a bon. Atoms bonds to acquire a stable outer shell, a stable configuration.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Ionic Bonds

A

Results from the transfer of electrons. An atom that gains electrons becomes an anion and an atom that loses an electron becomes a cation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Ions Necessary for Normal Nerve Function

A

Na+, Ca++, and Cl-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Ions Necessary for Normal Nerve Function

A

Na+, Ca++, and Cl-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Covalent Bonds

A

Form when atoms share electrons and the resulting structure is a molecule. Single covalent bonds results when two atoms share a pair of electrons; double occurs when two atoms share two pairs and so on.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Non-Polar Bond

A

Occurs when electrons are shared equally between two identical atoms. Found in diatomic molecules such as H2 or O2.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Polar Bonds

A

If electrons are shared unequally between two atoms.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Polar Bonds

A

If electrons are shared unequally between two atoms.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Polar and Non-Polar Molecules

A

Polar molecules are unbalanced and contain strong attractions. Non-Polar molecules are the opposite. Polar molecules will generally only dissolve in polar molecules and the opposite is true for non-polar molecules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Polar and Non-Polar Molecules

A

Polar molecules are unbalanced and contain strong attractions. Non-Polar molecules are the opposite. Polar molecules will generally only dissolve in polar molecules and the opposite is true for non-polar molecules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Hydrophobic and Hydrophilic

A

Substances that are polar will dissolve in water while substances that are non-polar will not. Lipids are hydrophobic and don’t dissolve in water this is the reason why oils separate when mixed with water. This is also the reason why only non-polar substances can pass through the plasma membrane. Large polar molecules must pass through hydrophilic protein channels.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

The Water Molecule

A

One side of the molecule has a negative charge (O) and one has a positive charge (H).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

The Water Molecule

A

One side of the molecule has a negative charge (O) and one has a positive charge (H). In addition, two molecules of water can be held together by hydrogen bonding.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Hydrogen Bonding

A

A weak bond created as a result of the electrostatic attraction between a negative molecule and a positive molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Specific Heat Definition

A

The amount of heat a substance must absorb to increase one gram of the substance by one degree celsius.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Water and Specific Heat

A

Water has a high specific heat and therefore, can provide a stable environmental temperature for the organisms that live there. In addition, because large bodies of water exhibit little temperature change, they moderate the climate of the nearby land.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Water and Vaporization

A

Water has a high heat of vaporization. This means that evaporating water required a relatively great amount of heat. As a result, the evaporation of sweat significantly cools the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Water as a Solvent

A

Since water is a highly polar molecule, it dissolves all polar and ionic substances.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Water and Tension

A

Water exhibits a very strong cohesion tension. This means that water molecules attract each other.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Transpirational-Pull Cohesion

A

Water moves up a tall tree from the roots to the leaves without the expenditure of energy due to water’s cohesion. As a molecules of water is lost from the leaves through transpiration another molecules is drawn in from the roots.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Capillary Action

A

Results from the combined forces of cohesion and adhesion.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Surface Tension

A

Allows insects to walk on water without breaking the surface. A result of cohesion.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Water as Ice

A

Ice floats because it is less dense than water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Spring Overturn

A

In the winter, ice allows the liquid under it to be insulated. Then, in the spring the ice melts and sinks to the bottom of the lake causing water to circulate. Oxygen is returned to the depths and nutrients from the bottom of the lake move upwards. The cycling of nutrients in the lake is know as spring overturn.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

pH Values

A

Anything less than a pH of 7 is an aid and anything over is basic/alkaline. 7 is a neutral pH. The value of pH is the negative log of the hydrogen ion concentration in moles per liter.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

pH of Stomach Acid

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

pH of Human Blood

A

7.4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

pH of Acid Rain

A

1.5-5.4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Internal pH of most living cells is…

A

about 7

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Buffer

A

Substances that resist changes in pH by absorbing excess hydrogen ions or donating hydrogen ions when there are too few.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Most Important Buffer in Human Blood

A

bicarbonate ion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

pH Values

A

Anything less than a pH of 7 is an aid and anything over is basic/alkaline. 7 is a neutral pH. The value of pH is the negative log of the hydrogen ion concentration in moles per liter. As H+ concentration increases pH decreases.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Most Important Buffer in Human Blood

A

bicarbonate ion - Donor/Acid: H2CO3; Acceptor/Base: HCO3-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Most Important Buffer in Human Blood

A

bicarbonate ion - Donor/Acid: H2CO3; Acceptor/Base: HCO3-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Isomer

A

Organic compounds that have the same molecular formula but different structure, therefore, different properties.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

Structural Isomers

A

Organic compounds that differ in arrangement of their atoms.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

Geometric Isomers

A

Organic compounds that differ only in spatial arrangements around double bonds which are not flexible like single bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

Optical Isomers or Enantiomers

A

Organic compounds that are mirror images of each other. The images are called the left-hand and the right-hand. Amino-acids are all left-handed.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Optical Isomers in Pharmaceuticals

A

Two mirror images of compounds may not be equally effective. L-dopa can treat Parkinson’s disease but R-dopa is useless in treatment of the disease.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Optical Isomers in Pharmaceuticals

A

Two mirror images of compounds may not be equally effective. L-dopa can treat Parkinson’s disease but R-dopa is useless in treatment of the disease.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Classes of Organic Compounds

A

carbohydrates, lipids, proteins and nucleic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Classes of Organic Compounds

A

carbohydrates, lipids, proteins and nucleic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

Carbohydrate Structure

A

Carbon, hydrogen and oxygen are the main three elements. The number of hydrogen atoms to the number oxygen atoms is 2 to 1. C(n)H(2)O is the empirical formula.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Carbohydrate Function

A

It is used in the body for quick energy. One gram of a carbohydrate will release 4 calories when it is burned.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Sources of Carbohydrates

A

Rice, pasta, bread, cookies, and candy are the dietary sources.

52
Q

Three Classes of Carbohydrates

A

monosaccharides, disaccharides and polysaccharides

53
Q

Monosaccharides

A

Chemical Formula: C6H12O6. Glucose, galactose and fructose are isomers of each other.

54
Q

Disaccharides

A

Chemical Formula: C12H22O11. They are formed by two monosaccharides joined when one molecule of water is released through dehydration synthesis/condensation.

55
Q

Dehydration Synthesis and Disaccharides

A

C6H12O6 + C6H12O6 = C12H22O11 + H2O

56
Q

Disaccharides

A

Chemical Formula: C12H22O11. Maltose, lactose and sucrose are examples. They are formed by dehydration synthesis/condensation.

57
Q

Dehydration Synthesis and Disaccharides

A

Two monosaccharides joined when one molecule of water is released. C6H12O6 + C6H12O6 = C12H22O11 + H2O

58
Q

Hydrolysis

A

The breakdown of a compound by adding water. The opposite of dehydration synthesis/condensation.

59
Q

Hydrolysis

A

The breakdown of a compound by adding water. The opposite of dehydration synthesis/condensation.

60
Q

Polysaccharides

A

Polymers of carbohydrates and are formed as many monosaccharides join together by dehydration synthesis. Important polysaccharides are cellulose, chitin, starch and glycogen.

61
Q

Cellulose as a Polysaccharide

A

Makes up plant cell walls.

62
Q

Starch as a Polysaccharide

A

Found in plants; two forms are amylose and amylopectin

63
Q

Chitin as a Polysaccharide

A

Makes up the exoskeleton in arthropods and cell walls in mushrooms.

64
Q

Glycogen

A

“Animal Starch”; In humans this is stored in the liver and skeletal muscle.

65
Q

Lipid Examples

A

They include fats, oils, waxes and steroids. They are grouped together because they are all hydrophobic and are not soluble in water.

66
Q

Lipid Structure

A

Consist of 1 glycerol and 3 fatty acids. Phospholipids are lipid molecules with a phosphate attached.

67
Q

Glycerol

A

Alcohol; C3H8O3

68
Q

Fatty Acid

A

A hydrocarbon chain with a carboxyl group at one end.

69
Q

Saturated

A

All the carbons are attached by single bonds to molecules. Saturated fats from animals are solids at room temperature and in large, ingested quantities may cause heart disease. (Ex. butter)

70
Q

Unsaturated

A

Carbons are attached by double bonds to molecules formed by the removal of hydrogen atoms in the carbon skeleton. In general, these are extracted from fats and are liquid at room temperature.

71
Q

Tropical Oils and their Saturation

A

Coconut oil and Palm oil are saturated, somewhat solid at room temperature and as unhealthy as animal fats. This contradicts the usual idea that plant oils are unsaturated and healthy at room temperature.

72
Q

Steroids

A

Lipids that consist of four fused rings. Examples are cholesterol, testosterone and estradiol.

73
Q

Lipid Functions

A

Energy storage; one gram of any lipid will release 9 calories per gram. Structural; a major component of the cell membrane such as the plasma membrane of animal cells. Endocrine; some steroids are hormones.

74
Q

Protein Function

A

Growth and repair; signaling from one cell to another; defense against invaders; catalyzing chemical reactions; etc..

75
Q

Protein Function

A

Growth and repair; signaling from one cell to another; defense against invaders; catalyzing chemical reactions; etc..

76
Q

Sources of Protein

A

fish, poultry, meat and certain plants such as beans and peanuts

77
Q

Protein Energy

A

one gram of a protein releases 4 calories

78
Q

Protein Structure

A

The main elements contained by a protein are Sulfur, Phosphorus, Carbon, Oxygen, Hydrogen and Nitrogen. They are polymers/polypeptides consisting of units called amino acids joined by peptide bonds.

79
Q

Amino Acid Structure

A

They consist of a carboxyl group (CHO2), an amine group (NH2) and a variable (R) attached to a central asymmetric carbon atom. The R group called the side chain differs with each amino acid. The 20 amino acids can build thousands of different proteins.

80
Q

Protein Conformation

A

Each protein has a unique shape that affects how it performs and functions. Four levels of protein structure a responsible for a protein’s unique conformation.

81
Q

Protein Conformation

A

Each protein has a unique shape that affects how it performs and functions. Four levels of protein structure a responsible for a protein’s unique conformation.

82
Q

Protein: Primary Structure

A

The unique linear sequence of amino acids. The slightest change can have dire consequences. Fred Sanger was the first to sequence the protein, insulin.

83
Q

Protein: Secondary Structure

A

The secondary structure of a protein results from hydrogen bonding within the polypeptide molecule. The polypeptide coils and folds into either an alpha helix of beta pleated sheets.

84
Q

Fibrous Proteins

A

Proteins that exhibit either alpha helix or pleated sheet. Examples are wool, claws, beaks, reptile scales, collagen and ligaments. The proteins that make up human hair is called keratin and is composed of alpha helixes.

85
Q

Protein: Tertiary Structure

A

The tertiary structure of a protein is the intricate three-dimensional shape of conformation of a protein that is superimposed on its secondary structure. This determines a protein’s specificity.

86
Q

Factors that Contribute to Tertiary Structure

A

Hydrogen bonding between R groups of amino acids; Ionic bonding between R groups; Hydrophobic interactions; Van de Waals interactions; Disulfide bonds between cysteine amino acids

87
Q

Protein: Quaternary Structure

A

The quaternary structure refers to proteins that consist of more than one polypeptide chain. Hemoglobin, for example, consists of four polypeptide chains each forming a heme group.

88
Q

The Protein-Folding Problem

A

The area of studying how proteins spontaneously folding into their unique shapes.

89
Q

Chaperone Proteins

A

Molecules that assist in folding other proteins.

90
Q

Chaperone Proteins

A

Molecules that assist in folding other proteins.

91
Q

The two Nucleic Acids

A

ribonucleic acid or deoxyribonucleic acid

92
Q

Nucleic Acid Structure

A

Repeating units called nucleotides make up nucleic acids.

93
Q

Nucleotide Structure

A

Consist sof a phosphate, a 5-carbon sugar (ribose/deoxyribose) and a nitrogenous base. Carbon atoms of deoxyribose are numbered from 1 to 5.

94
Q

Nitrogenous Bases

A

Adenine, Cytosine, Guanine and Thymine (DNA) or Uracil (RNA)

95
Q

Nitrogenous Bases

A

Adenine, Cytosine, Guanine and Thymine (DNA) or Uracil (RNA)

96
Q

Functional Groups

A

Components of organic molecules that are most often involved in chemical reactions. They are attached to the carbon skeleton and replace one or more hydrogen atoms.

97
Q

Functional Group - Amino

A

NH2; Name of Compound: Amine

98
Q

Functional Group - Carboxyl

A

COOH; Name of Compound: Carboxyl

99
Q

Functional Group - Hydroxyl

A

OH; Name of Compound: Alcohol

100
Q

Functional Group - Phosphate

A

PO4 (3-); Name of Comound: Organic Phosphate

101
Q

Functional Group - Phosphate

A

PO4 (3-); Name of Compound: Organic Phosphate

102
Q

First Law of Thermodynamics (Law of Conservation of Energy)

A

Energy cannot be created nor destroyed only transferred.

103
Q

Second Law of Thermodynamics

A

In the course of energy conversions the universe becomes more disordered (greater entropy).

104
Q

Gibb’s Free Energy

A 
ΔG = ΔH - TΔS
ΔG - change in free energy
ΔH - change in heat content
T - absolute temperature
ΔS - change in entropy
105
Q

Negative ΔG

A

Energy releasing reactions. Exergonic or exothermic.

106
Q

Positive ΔG

A

Energy absorbing equations. Endergonic or endothermic.

107
Q

Coupled Chemical Reactions

A

Cellular reactions in which the exergonic reactions power the endergonic ones.

108
Q

Metabolism

A

The sum of all the chemical reaction that take place in cells. Metabolic reactions controlled by enzymes that take place through pathways that serve a special function an are controlled by enzymes.

109
Q

Catabolism and Anabolism

A

Reactions that break down molecules or build them up.

110
Q

Enzymes

A

Serve as catalytic proteins that speed up reactions by lowering the energy of activation.

111
Q

Energy of Activation

A

The amount of energy needed to begin a reaction.

112
Q

Negative ΔG

A

Energy releasing reactions. Exergonic or exothermic. In a potential energy diagram the potential energy of the products is less than the potential energy of the reactions so the reaction is exothermic.

113
Q

Positive ΔG

A

Energy absorbing equations. Endergonic or endothermic. In a potential energy diagram the potential energy of the products is greater than the potential energy of the reactants.

114
Q

Enzymes

A

Globular proteins that exhibit tertiary structure; They serve as catalytic proteins that speed up reactions by lowering the energy of activation. Dotted lines on a potential energy diagram represent catalysts. Enzymes can catalyze in both directions.

115
Q

Energy of Activation

A

The amount of energy needed to begin a reaction.

116
Q

Induced-Fit Model

A

As a substrate enters an active site, it induces the enzymes to alter its shape slightly so the substrate fits better.

117
Q

Enzymes and Substrates

A

Enzymes are substrate specific. They are named after their substrate and the name ends in the suffix “ase”.

118
Q

Cofactors/Coenzymes

A

Cofactors are inorganic molecules that help enzymes and coenzymes are vitamins that help enzymes.

119
Q

Enzyme Efficiency

A

Enzymes are affected by pH and temperature. 37 degrees celsius is optimal for human enzymes. If temperature is too high enzymes denature and lose their conformation. Gastric enzymes becomes active at low pH while intestinal amylase works best in alkaline environments.

120
Q

Competitive Inhibition

A

Inhibition of an enzyme due to some compounds resemble the normal substrate molecule and compete for the same active site on the enzyme. These mimics reduce the productivity of enzymes by preventing the substrate from combining with an enzyme. They can be reversible or nonreversible.

121
Q

Noncompetitive Inhibition

A

When an enzyme contains more than one active site and the substrates do not resemble each other. Binding of either substrate presents the other from binding to the enzyme. The substrate that binds to the enzyme is ransom and a function of the concentration of each substrate.

122
Q

Noncompetitive Inhibition: Operon

A

The binding of a repressor to the operator on the DNA strand blocks the binding site for RNA polymerase and no transcription can occur.

123
Q

Allosteric Inhibition

A

Two active sites are present; one for a substrate and one for an inhibitor. The enzyme oscillates between two conformations; active or inactive. When the inhibitor binds the substrate site is altered and the enzyme cannot catalyze the reaction.

124
Q

Allosteric Inhibition: phosphofructokinase

A

Catalyzes step three in the production of pyruvic acid and is inhibited by ATP. This is an example of feedback inhibition where a metabolic pathway is switched off by its end product.

125
Q

Cooperativity

A

Substrates can stimulate an enzyme with quaternary structure to be more effective. For example, when oxygen bing to hemoglobin it can rapidly bind to three more oxygen atoms.

AP Biology (15 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions