Chapter 3 Flashcards

1
Q

nucleic acids

A

polymers that store, transmit, and express heredity information

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

DNA

A

deoxyribonucleic acid, stores and transmits genetic information

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

RNA

A

specify the amino acid sequences of proteins

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

nucleotides

A

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

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

nucleosides

A

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

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

pyrimidine

A

six-membered single-ring structure of the base

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

purine

A

fused double-ring structure of the base

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

What is the difference between deoxyribose and ribose?

A

Ribose has one more oxygen atom

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

phosphodiester bond

A

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

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

oligonucleotides

A

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

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

polynucleotides

A

DNA

most RNA

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

What are the bases found in DNA?

A

adenine
cytosine
guanine
thymine

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

What are the bases found in RNA?

A

adenine
cytosine
guanine
uracil

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

What are the complementary base pairs for DNA?

A

A-T

C-G

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

What are the complementary base pairs for RNA?

A

A-U

C-G

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

What intermolecular force holds together base pairs?

A

hydrogen bonds

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

Describe the structure of RNA

A

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

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

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

DNA replication

A

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

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

tnanscription

A

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

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

translation

A

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

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

genes

A

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

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

genome

A

complete set of DNA in a living organism

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

enzymes

A

catalytic molecules that speed up biochemical reactions, typically proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
defensive proteins
recognize and respond to substance of particles that invade the organism from the environment
26
hormonal and regulatory proteins
control physiological processes
27
receptor proteins
receive and respond to molecular signals
28
storage proteins
store chemical building blocks for later use
29
structural proteins
provide physical stability and enable movement
30
transport proteins
carry substances without the organism
31
genetic regulatory proteins
transcription factors, regulate when, how, and to what extent a gene is expressed
32
proteins
polymers made up of amino acids
33
What are the functional groups found in amino acids?
nitrogen-containing amino group and acidic carboxyl group
34
R group
also known as side chain, this distinguishes each of the amino acids
35
disulfide bridge
covalent bond between sulfurs on side chains
36
oligopeptides
can just be referred to as peptides, these are short polymers of 20 or fewer amino acids
37
polypeptides
longer polymers with unique sequences of amino acids
38
peptide bond
between the amino group of one amino acid and the carboxyl group of another after a condensation reaction occurs
39
primary structure
precise sequence of amino acids in a polypeptide chain
40
secondary structure
consists of regular, repeated patterns in different regions along the polypeptide chain ~alpha helix ~beta pleated sheet
41
alpha helix
right-handed coil, as a result of hydrogen bonds between N-H group and C=O group
42
beta pleated sheet
sequences of amino acids that are extended and aligned, can form between different polypeptide chains or a single chain folded on itself
43
tertiary structure
results in the polypeptide's three-dimensional shape, as a result of interactions between R groups
44
denatured
secondary and tertiary structures break down due to heating
45
quarternary structure
results from the ways in which the subunits bind together and interact
46
What is the effect of temperature increases on protein structure?
cause more rapid molecular movements and thus can break hydrogen bonds and hydrophobic interactions
47
What is the effect of pH changes on protein structure?
can change the patterns of ionization of the exposed carboxyl and amino groups. This can disrupt the patterns of ionic attractions and repulsions
48
What is the effect of high concentrations of polar substances on protein structure?
disrupt the hydrogen bonding that is crucial to protein structure
49
What is the effect of nonpolar substances on protein structure?
may also denature a protein in cases where hydrophobic groups are essential for maintaining the protein's structure
50
catalyst
speeds up the reaction without altering it by lowering the activation energy, can be reused DOES NOT CAUSE THE REACTION TO OCCUR
51
enzymes
biological catalysts (mostly proteins, but some are RNA)
52
free energy (G)
amount of energy in a system that is available to do work, released by an exergonic reaction
53
transition state
reactive mode after an input of energy (peak of graph)
54
activation energy
energy input to reach the transition state
55
substrates
the reactants in an enzyme-catalyzed reaction
56
active site
particular site on the enzyme where catalysis takes place
57
What contributes to the specificity of an enzyme?
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
Enzyme-Substrate Complex
binding of a substrate to the active site of an enzyme
59
What is the general form of an enzyme-substrate reaction?
E + S --> ES --> E + P
60
inducing strain
enzyme causes bonds in the substrate to stretch, putting it in an unstable state
61
substrate orientation
brings together specific atoms so that bonds can form
62
adding chemical groups
R groups of an enzyme may be directly involved in the reaction
63
What are the roles of the rest of the enzyme macromolecule?
~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
cofactors
ions or other molecules that certain enzymes need in order to function
65
What are the three categories of cofactors?
~metal ions ~coenzymes ~prosthetic groups
66
metal ions
bind to certain enzymes and participate in the enzyme-catalyzed reactions
67
coenzyme
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
prosthetic groups
organic molecules that are permanently bound to their enzymes
69
metabolic pathways
product of one reaction is the substrate for the next
70
systems biology
scientists describe mathematically the components of metabolic systems
71
Why do cells need to regulate their metabolic pathways?
so that they can respond to changes either within the organism or in its environment
72
How could a cell regulate metabolism?
~control the amount of an enzyme | ~regulate the activity of enzymes
73
competitive inhibitor
competes with the natural substrate for the active site, it is reversible
74
noncompetitive inhibitor
binds to an enzyme at a site distinct from the active site, it is reversible
75
allosteric regulation
non-substrate molecule binds or modifies a site other than the active site of an enzyme
76
noncovalent binding (allosteric regulation)
causes the enzyme to change shape, is reversible, may result in the inactivation of an enzyme
77
covalent bonding (allosteric regulation)
when a molecule or chemical group binds to an allosteric site
78
feedback inhibition
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
What is the effect of temperature on a chemical reaction?
Generally increases the rate of the reaction, can result in protein denaturing at high temperatures
80
irreversible inhibition
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