Chapter 3 - Nucleic Acids, Proteins, and Enzymes Flashcards

(54 cards)

1
Q

if you were given a diagram of a nucleotide what you expect to find as its components

A

phosphate, sugar, and a base

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2
Q

how is DNA different than RNA

A

it contains deoxyribose

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3
Q

the observations that DNA with a higher G + C content is more stable at high temperatures than DNA with a high A+ T content because of what?

A

because each G and C pair forms three hydrogen bonds between antiparallel strands, whereas each A and T pair forms just two

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4
Q

replication is the synthesis of ____ and transcription is the synthesis of _____

A

an identical copy of DNA; an RNA template based on the DNA template

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5
Q

Quaternary structure of proteins refers to ____?

A

the number and kind of protein subunits the protein has

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6
Q

the binding of a substrate to an enzyme

A

may involve hydrogen bonds and van der waals interactions

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7
Q

in a reaction catalyzed by an enzyme

A

the enzyme does not affect the equilibrium constant for the reaction

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8
Q

a competitive inhibitor of an enzyme-catalyzed reaction

A

is usually similar to the substrate

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9
Q

the rate of a reaction catalyzed by an enzyme that has a single polypeptide chain

A

may be increase or decreased by temperature

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10
Q

enzymes

A

may be subject to feedback inhibition

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11
Q

what are nucleic acids

A

palmers that store, transmit, and express hereditary information

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12
Q

two things proteins are essential for

A

metabolism and structure

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13
Q

pyrimidine

A

six membered single ring structure

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14
Q

purine

A

fused double-ring structure

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15
Q

DNA sugar groups

A

Adenine
Cytosine
Guanine
Thymine

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16
Q

RNA sugar groups

A

Adenine
Cytosine
Guanine
Uracil

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17
Q

what makes the DNA structure less flexible than that of RNA

A

lack of a hydroxyl group at the 2’ position of the deoxyribose sugar

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18
Q

complementary base pairing

A
In DNA 
A-T
C-G
In RNA
A-U
C-G
held together primarily by hydrogen bonds
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19
Q

RNA characteristics

A

single stranded
can fold back on itself to form a double stranded helix
this folding occurs by complementary base pairing

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20
Q

DNA characteristics

A

double stranded
consists of two polynucleotide strands of the same length
strands are antiparallel: 5’ ends are at opposite ends of the double-stranded molecule
remarkably uniform
sugar-phosphate groups form the sides of the ladder and the bases with their hydrogen bonds form the rungs on the inside

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21
Q

genome

A

complete set of DNA in a living organism

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22
Q

Enzymes

A

catalytic molecules that speed up biochemical reactions. most enzymes are proteins (some are RNA molecules)

23
Q

Defensive proteins

A

such as antibodies recognize and respond to substances or particles that invade the organism from the environment

24
Q

peptide bonds

A

in the “backbone” of a protein are formed as covalent “peptide bonds” between adjacent amino acids.

25
hormonal and regulatory proteins
such as insulin control physiological processes
26
receptor proteins
receive and respond to molecular signals from inside and outside the organism
27
storage proteins
store chemical building blocks-- amino acids -- for later use.
28
Structural proteins
such as collagen provide physical stability and enable movement
29
transport proteins
such as hemoglobin carry substances within the organism
30
Genetic regulatory proteins
regulate when, how, and to what extent a gene is expressed
31
functions of proteins
``` enzymes structure defense signaling receptor membrane transport storage bulk transport gene regulation ```
32
what are the building blocks of proteins
amino acids
33
how can amino acids be classified
on the amino acids they posses
34
labels amino acids can receive
``` polar charged (hydrophilic) polar uncharged (hydrophilic) nonpolar (hydrophobic) ```
35
what functional groups do amino acids contain?
nitrogen containing amin group and the (acidic) carboxyl group
36
3 amino acids that are hydrophobic
glycine, proline, and cysteine
37
primary structure of a protein
is established by covalent bonds
38
____ of proteins are folded into 3D shapes
the polypeptide chains
39
secondary structure of a protein
consists of regular, repeated, spatial patterns in different regions of a polypeptide chain. alpha helix beta pleated sheet
40
tertiary structure of a protein
the polypeptide chain is bent at specific sites and then folded back and forth results in the polypeptides definitive three-dimensional shape
41
secondary and tertiary structures derive from ___
primary structure
42
quaternary structure of a protein
results from ways in which these subunits bind together and interact. Hemoglobin is an example of a protein with multiple subunits
43
catalyst
used to speed up a reaction without itself being permanently altered proteins that are enzymes speed up biochemical reactions, acting as biological catalysts that are highly specific for their substrates
44
substrate
name for reactants in a enzyme-catalyzed reaction
45
an enzymes active site determines its ____
specificity
46
active site
where the substrate molecule binds to the enzyme
47
irreversible inhibition
if an inhibitor covalently binds to an amino acid side chain at the active site of an enzyme, the enzyme if permanently inactivated because it cannot interact with its substrate. EX: DIPF (diisoprpyl phosphorofluoridate)
48
reversible inhibition
an inhibitor is similar enough to a particular enzyme's natural substrate that is can bind noncovalently to the active site, yet different enough that no chemical reaction occurs analogus to a key that inserts into a lock but does not turn it
49
competitive inhibitor
when a molecule competes with the natural substrate for the active site
50
noncompetitive inhibitor
binds to an enzyme at a site distance from the active site. this binding causes a change in the shape of the enzyme, altering its activity.
51
allosteric regulation
occurs when a non-substrate molecule binds or modifies a site other than the active site of an enzyme
52
the activity of allosteric enzyme complexes results from what
the activity of both positive and negative regulators
53
what effects enzyme activity
temperature and ph
54
feedback inhibition
when the end product is present at a high concentration, some of it binds to a site on the commitment step enzyme, thereby causing it to become inactive