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AP Biology > Chapter 3 > Flashcards

Chapter 3 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

nucleic acids

A

polymers that store, transmit, and express heredity information

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2
Q

DNA

A

deoxyribonucleic acid, stores and transmits genetic information

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3
Q

RNA

A

specify the amino acid sequences of proteins

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4
Q

nucleotides

A

the monomers of nucleic acids consisting of three components: nitrogen-containing base, pentose sugar, one to three phosphate groups

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5
Q

nucleosides

A

consists of pentose sugar and a base, but no phosphate group

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6
Q

pyrimidine

A

six-membered single-ring structure of the base

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7
Q

purine

A

fused double-ring structure of the base

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8
Q

What is the difference between deoxyribose and ribose?

A

Ribose has one more oxygen atom

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9
Q

phosphodiester bond

A

linkage between the pentose sugar of one nucleotide and the phosphate of another nucleotide after a condensation reaction

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10
Q

oligonucleotides

A

RNA: begin duplication of DNA, regulate gene expression
DNA: amplifying and analysing other nucleotide sequences

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11
Q

polynucleotides

A

DNA

most RNA

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12
Q

What are the bases found in DNA?

A

adenine
cytosine
guanine
thymine

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13
Q

What are the bases found in RNA?

A

adenine
cytosine
guanine
uracil

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14
Q

What are the complementary base pairs for DNA?

A

A-T

C-G

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15
Q

What are the complementary base pairs for RNA?

A

A-U

C-G

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16
Q

What intermolecular force holds together base pairs?

A

hydrogen bonds

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17
Q

Describe the structure of RNA

A

usually single-stranded, but it can fold on itself to attain a three dimensional structure

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18
Q

Describe the structure of DNA

A

two separate polynucleotide strands which are antiparallel, twists into a double helix, typically a right handed molecule

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19
Q

DNA replication

A

precise reproduction through polymerization using an existing strand as a base-pairing template

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20
Q

tnanscription

A

Information coded in the sequence of nucleotide bases in DNA is passed to a sequence of nucleotide bases in RNA

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21
Q

translation

A

Information in RNA is passed to polypeptides, but never the reverse

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22
Q

genes

A

sequences of DNA that encode specific proteins and are transcribed into RNA

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23
Q

genome

A

complete set of DNA in a living organism

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24
Q

enzymes

A

catalytic molecules that speed up biochemical reactions, typically proteins

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25
Q

defensive proteins

A

recognize and respond to substance of particles that invade the organism from the environment

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26
Q

hormonal and regulatory proteins

A

control physiological processes

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27
Q

receptor proteins

A

receive and respond to molecular signals

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28
Q

storage proteins

A

store chemical building blocks for later use

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29
Q

structural proteins

A

provide physical stability and enable movement

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30
Q

transport proteins

A

carry substances without the organism

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31
Q

genetic regulatory proteins

A

transcription factors, regulate when, how, and to what extent a gene is expressed

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32
Q

proteins

A

polymers made up of amino acids

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33
Q

What are the functional groups found in amino acids?

A

nitrogen-containing amino group and acidic carboxyl group

34
Q

R group

A

also known as side chain, this distinguishes each of the amino acids

35
Q

disulfide bridge

A

covalent bond between sulfurs on side chains

36
Q

oligopeptides

A

can just be referred to as peptides, these are short polymers of 20 or fewer amino acids

37
Q

polypeptides

A

longer polymers with unique sequences of amino acids

38
Q

peptide bond

A

between the amino group of one amino acid and the carboxyl group of another after a condensation reaction occurs

39
Q

primary structure

A

precise sequence of amino acids in a polypeptide chain

40
Q

secondary structure

A

consists of regular, repeated patterns in different regions along the polypeptide chain
~alpha helix
~beta pleated sheet

41
Q

alpha helix

A

right-handed coil, as a result of hydrogen bonds between N-H group and C=O group

42
Q

beta pleated sheet

A

sequences of amino acids that are extended and aligned, can form between different polypeptide chains or a single chain folded on itself

43
Q

tertiary structure

A

results in the polypeptide’s three-dimensional shape, as a result of interactions between R groups

44
Q

denatured

A

secondary and tertiary structures break down due to heating

45
Q

quarternary structure

A

results from the ways in which the subunits bind together and interact

46
Q

What is the effect of temperature increases on protein structure?

A

cause more rapid molecular movements and thus can break hydrogen bonds and hydrophobic interactions

47
Q

What is the effect of pH changes on protein structure?

A

can change the patterns of ionization of the exposed carboxyl and amino groups. This can disrupt the patterns of ionic attractions and repulsions

48
Q

What is the effect of high concentrations of polar substances on protein structure?

A

disrupt the hydrogen bonding that is crucial to protein structure

49
Q

What is the effect of nonpolar substances on protein structure?

A

may also denature a protein in cases where hydrophobic groups are essential for maintaining the protein’s structure

50
Q

catalyst

A

speeds up the reaction without altering it by lowering the activation energy, can be reused
DOES NOT CAUSE THE REACTION TO OCCUR

51
Q

enzymes

A

biological catalysts (mostly proteins, but some are RNA)

52
Q

free energy (G)

A

amount of energy in a system that is available to do work, released by an exergonic reaction

53
Q

transition state

A

reactive mode after an input of energy (peak of graph)

54
Q

activation energy

A

energy input to reach the transition state

55
Q

substrates

A

the reactants in an enzyme-catalyzed reaction

56
Q

active site

A

particular site on the enzyme where catalysis takes place

57
Q

What contributes to the specificity of an enzyme?

A

The exact three dimensional shape, or conformation, and chemical properties of the active site make it so that only substrates with certain shapes, functional groups, and chemical properties can bind to the enzyme.

58
Q

Enzyme-Substrate Complex

A

binding of a substrate to the active site of an enzyme

59
Q

What is the general form of an enzyme-substrate reaction?

A

E + S –> ES –> E + P

60
Q

inducing strain

A

enzyme causes bonds in the substrate to stretch, putting it in an unstable state

61
Q

substrate orientation

A

brings together specific atoms so that bonds can form

62
Q

adding chemical groups

A

R groups of an enzyme may be directly involved in the reaction

63
Q

What are the roles of the rest of the enzyme macromolecule?

A

~provides a framework so the amino acids of the active site are properly positioned in relation to the substrate
~participates in the changes in protein shape and structure that result in induced fit
~provides binding sites for regulatory molecules

64
Q

cofactors

A

ions or other molecules that certain enzymes need in order to function

65
Q

What are the three categories of cofactors?

A

~metal ions
~coenzymes
~prosthetic groups

66
Q

metal ions

A

bind to certain enzymes and participate in the enzyme-catalyzed reactions

67
Q

coenzyme

A

a relatively small, carbon-containing molecule required for the action of one or more enzymes. It binds to the active site of the enzyme, adds or removes a chemical group from the substrate, and then separates from the enzyme to participate in other reactions

68
Q

prosthetic groups

A

organic molecules that are permanently bound to their enzymes

69
Q

metabolic pathways

A

product of one reaction is the substrate for the next

70
Q

systems biology

A

scientists describe mathematically the components of metabolic systems

71
Q

Why do cells need to regulate their metabolic pathways?

A

so that they can respond to changes either within the organism or in its environment

72
Q

How could a cell regulate metabolism?

A

~control the amount of an enzyme

~regulate the activity of enzymes

73
Q

competitive inhibitor

A

competes with the natural substrate for the active site, it is reversible

74
Q

noncompetitive inhibitor

A

binds to an enzyme at a site distinct from the active site, it is reversible

75
Q

allosteric regulation

A

non-substrate molecule binds or modifies a site other than the active site of an enzyme

76
Q

noncovalent binding (allosteric regulation)

A

causes the enzyme to change shape, is reversible, may result in the inactivation of an enzyme

77
Q

covalent bonding (allosteric regulation)

A

when a molecule or chemical group binds to an allosteric site

78
Q

feedback inhibition

A

when the end product is present at a high concentration, some of it binds to a site (active or allosteric) on the commitment step enzyme, causing it to become inactive

79
Q

What is the effect of temperature on a chemical reaction?

A

Generally increases the rate of the reaction, can result in protein denaturing at high temperatures

80
Q

irreversible inhibition

A

occurs when an inhibitor covalently binds to an amino acid side chain at the active site of an enzyme, so the enzyme is permanently inactivated

AP Biology (19 decks)

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