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AP Biology > Biochemistry > Flashcards

Biochemistry Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Proton

A

● Subatomic particles inside an atom

● Relatively positive charge

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2
Q

Neutron

A

● Subatomic particles inside an atom

● Neutral in charge

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3
Q

Electron

A

● Subatomic particles inside an atom

● Negative charge

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4
Q

Ground state

A

When all the electrons in an atom are in the lowest available energy levels

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5
Q

Excited state

A

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

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6
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

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7
Q

Half-life

A

Amount of time needed to convert 50% of the parent compound into daughter compound

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8
Q

Radioisotopes

A

● Radioactive isotopes

● Used in medicine and dating

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9
Q

Tracer

A

Can be incorporated into a molecule and used to trace the path of carbon dioxide in a metabolic pathway

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10
Q

Ionic bonds

A

Result from the transfer of electrons

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11
Q

Anion

A

A negative ion

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12
Q

Cation

A

A positive ion

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13
Q

Covalent bonds

A

Form when atoms share electrons

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14
Q

Nonpolar

A

When electrons are shared equally between two atoms

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15
Q

Diatomic molecules

A

Two identical atoms form a nonpolar covalent bond

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16
Q

Polar

A

When electrons are shared unequally between two atoms

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17
Q

Hydrophobic

A

● Water hating

● Nonpolar and lipid-soluble

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18
Q

Hydrophilic

A

● Water loving

● Include substances that are polar or that carry a charge or that are ionic

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19
Q

Hydrogen bonds

A

Bonds formed between two water molecules

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20
Q

Specific heat

A

Amount of heat a substance must absorb to increase 1 gram of the substance by 1 degree

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21
Q

Transpirational-pull cohesion tension

A

● As one molecule of water is lost from the leaf by transpiration, another molecule is drawn in at the roots
● One of the way to move water molecules up

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22
Q

Capillary action

A

● Combined forces of cohesion and adhesion

● Water moves up a thin tube

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23
Q

Surface tension

A

● Hydrogen bonds are slightly stronger on the surface of water
● Allows insects to walk on water without breaking the surface

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24
Q

Spring overturn

A

● The cycling of the nutrients in the lake
● Oxygen from the surface is returned to the depths, and nutrients released by the activities of bottom-dwelling bacteria during winter are carried to the upper layers of the lake

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25
Q

pH

A

● A measure of the acidity and alkalinity of a solution
● Ranges from 1 - 14
- 7 is neutral
● pH = - log [H+]

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26
Q

Buffer

A

● Substances that resist changes in pH
● It works by either absorbing excess hydrogen ions or donating hydrogen ions when there are too few
● The most important buffer in human blood is the bicarbonate ion

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27
Q

Isomers

A

Organic compounds that have the same molecular formula but different structures

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28
Q

Structural isomers

A

Differ in the arrangement of their atoms

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29
Q

Cis-trans isomers

A

Differ onl in spatial arrangement around double bonds, which are not flexible like single bonds are

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30
Q

Enantiomers

A

● Molecules that are mirror images of each other

● L- (left-handed) D- (right-handed)

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31
Q

Organic compounds

A

Compounds that contain carbon

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32
Q

Carbohydrates

A

● The body uses them for fuel and as building materials

● Consist of three elements – carbon, hydrogen, oxygen

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33
Q

Lipids

A

● Hydrophobic organic compounds that include fats, oils, waxes, and steroids
● Most lipids consist of 1 glycerol and 3 fatty acids
Functions
● Energy storage – 1 gram lipid = 9 calories
● Structural – phospholipids, cholesterol
● Endocrine

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34
Q

Proteins

A

● Complex, unbranhced macromolecules
Functions
● Growth and repair
● Signaling from one cell to another
● Regulation – hormones such as insulin lower blood sugar
● Enzymatic acivity – catalyzing chemical reactions
● Movement – actin and myosin are protein fibers responsible for muscle contractions

35
Q

Nucleic Acids

A

● Encode all hereditary information

● Include ribonucleic acid (RNA) and deoxyribonucleic acid (DNA)

36
Q

Dehydration synthesis

A

Release of one molecule of water to form polymers

37
Q

Hydroalysis

A

Breakdown of a compound by adding water

38
Q

Monosaccharides

A

● Monomer of carbohydrates
● Have a chemical formula of C6H12O6
● Three examples are glucose, galactose, and fructose

39
Q

Disaccharides

A

● Consist of two monosaccharides joined together

● Have the chemical formula C12H22O11

40
Q

Polysaccharides

A

● Polymer of carbohydrates
● Macromolecules
● Formed as many monosaccharides joined together
● Cellulose and starch are found in plants
● Chitin and glycogen are found in animals

41
Q

Glycerol

A

An alcohol that makes up the “head” of lipids

42
Q

Fatty acid

A

● Hydrocarbon chain with a carboxyl group at one end

● Exist in two varieties, saturated and unsaturated

43
Q

Saturated fatty acid

A

● Come from animals
● Solid at room temperature
● Linked to heart disease when ingested in large quantities
● Butter
● Contain only single bonds between carbon atoms

44
Q

Unsaturated fatty acid

A

● Extracted from plants
● Liquid at room temperature
● Considered to be healthy dietary fats
● Have at least one double bond formed by the removal of hydrogen atoms in the carbon skeleton
● They hold fewer hydrogen atoms than saturated fatty acids

45
Q

Steroids

A

● Lipid that do not have the same general structure as other lipids
● Consist of four fused rings
● Cholesterol, testosterone, estradiol

46
Q

Phospholipids

A

● Modified lipids
● Consist of only two fatty acids attached to the glycerol backbone, forming two hydrophobic “tails”
● The thrid hydroxyl group of the glycerol attaches to a phosphate group, which is charged and therefore hydrophilic
● Phospholipid bilayer is the structural basis of all plasma membranes

47
Q

Amino acids

A

● Monomer of proteins
● Consist of a carboxyl group, an amine group, and a variable (R) all attached to a central asymmetric carbon atom
- The R group differs with each amino acid

48
Q

Peptide bonds

A

Bonds that join amino acids together to form polymers of proteins

49
Q

Primary structure of proteins

A

The unique linear sequence of amino acids

50
Q

Secondary structure of proteins

A

● Results from hydrogen bonding with the polypeptide molecule
● Refers to how the polypeptide coils or folds into two distinct shapes – an alpha helix or a beta pleated sheet
- Peptide bond and hydrogen bond

51
Q

Tertiary structure of proteins

A

● Intricate 3-D shape of a protein that is superimposed on its secondary structure
● Determines the protein’s specificity

52
Q

Quaternary structure of proteins

A

Proteins that consist of more than one polypeptide chain

53
Q

Fibrous proteins

A

Proteins that exhibit either alpha helix or beta pleated sheet or both

54
Q

Denaturation

A

Lost of a protein’s characteristic shape as well as its function

55
Q

Conformation

A

Unique shape of each protein that determines what job it performs and how it functions

56
Q

Chaperone protiens/Chaperonins

A

Molecules that assist in folding other proteins

57
Q

Prions

A

Misfolded proteins

58
Q

Nucleotides

A

● Monomer of nucleic acids

● Consists of a phosphate (P), a 5-carbon sugar (deoxyribose/ribose), and a nitrogen base

59
Q

Function groups

A

● The components of organic molecules that are most often involved in chemical reactions
● These groups are attached to the carbon skeleton, replacing one or more hydrogen atoms that would be presnet in hydrocarbon

60
Q

First law of thermodynamics

A

● States that energy cannot be created or destroyed, only transformed from one form to another
● Often known as the law of conservation of energy

61
Q

Second law of thermodynamics

A

States that during energy conversions, the universe becomes more disordered

62
Q

Gibb’s free energy

A

Free energy, represented by the letter G

63
Q

Exergonic

A

If energy is released during the course of a reaction, the reaction is exergonic or exothermid and change is G is negative

64
Q

Endergonic

A

If in a chemical reaction energy is absorbed, the reaction is endergonia or endotehrmic and change in G is positive

65
Q

Metabolism

A

The sum of all the chemical reactions that take place in cells

66
Q

Catabolism

A

Reactions that break down molecules and release energy

67
Q

Anabolism

A

Reations that build up molecules and absorb energy

68
Q

Enzymes

A 
● Serve as catalytic proteins that speed up reactions by lowering the energy of activation
● Made up of protein
● Substrate specific
● Can be reused after a reaction
● Catalyze reactions in both directions
69
Q

Energy of activation

A

The amount of energy needed to begin a reaction

70
Q

Transition state

A

The reactive (unstable) condition of the substrate after sufficient energy has been absorbed to initiate the reaction

71
Q

Induced-fit model

A

● Describes how enzymes work
● As the substrate enters the active site, it induces the enzyme to alter its shape slightly so the substrate fits better

72
Q

Cofactors

A

Inorganic molecules that help enzyme’s functions

73
Q

Coenzymes

A

Organic molecules that help enzyme’s functions

74
Q

Competitve inhibitors

A

● Compounds that resemble the substrate molecules and compete for the same active site on the enzyme
● They reduce the amount of product by preventing or limiting the substrate from binding to the enzyme
● Can be overcome by increasing the concentration of substarte

75
Q

Allosteric regulators/noncompetitve inhibitors

A

● Bind to a site distinct and separate from the active site of the enzyme
● This binding of the inhibitor to the alternate site causes the enzyme to change shape in a way that inhibits the enzme from catalyzing substrate into product

76
Q

Feedback inhibition

A

The end product of the pathway is the allosteric inhibitor for an enzyme that catalyzes an early step in the pathway

77
Q

Cooperativity

A

● A type of allosteric activation
● The binding of one substrate molecule to one active site of one subunit of hte enzyme causes a change in the entire molecule and locks all subunits in an active position
● This mechanism amplifies the response of an enzume to its substrates

78
Q

What happened to the energy when a bond is formed? Why?

A

● Energy is released

● Atoms acquire a more stable configuration by completing their outer shell

79
Q

What is required to break a bond?

A

Energy must be supplied

80
Q

What are the five intramolecular factors that contribute to the tertiary structure?

A

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

81
Q

What does protein structure depend on?

A 
● The primary structure of a protein
● Physical and chemical consditions in the environment
- pH
- Salt concentration
- Temperature
82
Q

What are the three complementary techiniques that are used to reveal the 3D shape of proteins?

A

● X-ray crystallography
● Nuclear magnetic resonance (NMR) spectroscopy
● Bioinformatics

83
Q

What are the four nitrogen bases?

A

● Adenine (A)
● Cytosine (C)
● Guanine (G)
● Thymine (T) / Uracil (U)

84
Q

What are the four ways to regurate enzymes?

A

● Competitive inhibitors
● Allosteric inhibitors
● Feedback inhibition
● Cooperativity

AP Biology (15 decks)

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