Cell Biology Exam 1

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92 Terms

1
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What makes up a single deoxyribonucleotide?

A molecule of the 5-carbon sugar deoxyribose, a nitrogenous base, and a phosphate group

2
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If you want to see the smallest detail on the outside of a cell, what is the best type of microscope to use?

Scanning electron microscope

3
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What are membrane bound compartments within cells?

organelles

4
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Where are organelles found?

in all plant and animal cells

5
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is the nucleus an organelle?

yes

6
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what is true for organelles?

they can have different pH and other environmental features from the cytoplasm

7
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What is present in plant cells but NOT in animal cells?

Chloroplast and Central vacuole

8
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What chemical bond results from sharing of electrons so they orbit both atoms in the bond?

covalent bonds

9
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What are the charges of THR (Threonine), TYR (Tyrosine), SER (serine), GLN (Glutamine), ASN (Asparagine)?

uncharged polar amino acids

10
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what are the charges of ALA (Alanine), GLY (Glycine), VAL (valine), LEU (leucine), ILE (Isoleucine), PRO (Proline), PHE (Phenylalanine), MET (Methionine), TRP (Tryptophan), CYS (Cystine)?

nonpolar amino acids

11
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what are the charges of ARG (Arginine), LYS (Lysine), and HIS (Histidine)?

positively charged polar amino acids (basic)

12
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most enzymes are?

proteins

13
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what type of catalytic activity do enzymes have?

they are catalysts

14
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how do enzymes bind their substrate?

using the active site

15
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how are some enzymes regulated?

using a regulatory molecule and an allosteric site

16
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what happens according to the induced fit model for enzyme activity?

the substrate binding to the enzyme active site causes a shape change allowing the enzyme to better interact with the substrate

17
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When GTP is bound, the protein is

activated

18
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When GDP is bound, the protein is

inactivated

19
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why are enzymes called catalysts of biochemical reactions?

because they reduce the activation energy of a reaction

20
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what is an example of a fibrous protein?

fibroin

21
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what is an example of a globular protein?

hemoglobin

22
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T/F: the binding site for a ligand or substrate is formed from adjacent amino acids in the polypeptide chain

false

23
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what is an enzyme that breaks down proteins called?

protease

24
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what is an enzyme that breaks down nucleic acids is called a?

nuclease

25
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<p>where is the carboxyl end of the polypeptide?</p>

where is the carboxyl end of the polypeptide?

e

26
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<p>Where is the amino acid end of the polypeptide?</p>

Where is the amino acid end of the polypeptide?

b

27
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<p>where is the peptide bond located?</p>

where is the peptide bond located?

c

28
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<p>how many amino acids are chained together here?</p>

how many amino acids are chained together here?

3

29
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what is a cell?

the fundamental unit of life and basic structure (lowest level of organization that can perform all activities required for life)

30
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what are nucleotides?

building blocks for DNA and RNA

31
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what are the building blocks for proteins?

Amino acids

32
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what carries genetic information?

DNA

33
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what is replication?

the process of DNA synthesis

34
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what is transcription?

RNA synthesis

35
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what is translation?

protein synthesis

36
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what is transmission electron microscopy?

electrons are transmitted through the interior of the specimen

37
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what is scanning electron microscopy?

when the surface of a specimen is scanned by detecting electrons deflected from the outer surface

38
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bacteria and archaea are?

prokaryotes

39
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what do prokaryotes lack?

membrane bound organelles, nucleus

40
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what is something prokaryotes have that eukaryotes lack?

cell wall

41
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what is a plant cell wall made up of?

cellulose

42
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what is brightfield light microscopy?

differential interference contrast

43
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what is rough ER?

flattened form of endoplasmic reticulum

44
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what is the smooth ER?

tubular form of ER

45
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what does the rough ER do?

protein synthesis

46
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what does the smooth ER do?

site of lipid synthesis and membrane assembly

47
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what does the golgi apparatus do?

receives and modifies molecules from the ER and sends them in or out of the cell

48
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where are sugars added to proteins?

golgi apparatus

49
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what do lysosomes do?

digest biomolecules

50
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what transports components throughout cells?

small vesicles

51
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what is responsible for muscle contraction?

actin

52
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what type of bond receives and gives electrons between adjacent atoms?

ionic bond

53
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what is a hydrogen bond?

weak bonds between a slight positive hydrogen and slight negative atom

54
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what is a polar covalent bond

the sharing of atoms between two molecules where one atom is more electronegative, so the sharing is unequal (slight +/-).

55
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what is the amino acid formula?

amino groups, alpha carbon atom, carboxyl group, r side chain

56
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what charge do ASP (Aspartic acid), and GLU (glutamic acid have?

(acidic) negative charge

57
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what is the structure of a nucleotide?

a five-sugar base attached to a phosphate group and a nitrogenous base

58
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what bases are different in RNA and DNA?

Thymine (DNA) and Uracil (RNA)

59
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what are the functions of proteins?

catalyze chemical reactions, provide structural support, regulate membrane permeability

60
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how do amino acids chain together

within a protein, linked by peptide bonds

61
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what is primary structure?

amino acid sequence

62
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what is secondary structure?

folding into alpha helix and beta sheets

63
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what is tertiary structure?

3D folding of a single polypeptide chain

64
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what is quaternary structure?

multiple polypeptides forming

65
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what are cofactors?

protein components needed for protein function

66
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what is another word for ligand?

substrate

67
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what are globular proteins?

folded into compact tertiary sstructures

68
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what are fibrous proteins

extensive regions of secondary structures that are given a highly ordered repetitive structured

69
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what are allosteric proteins?

can cause shape change and can either help site function or prevent it

70
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what is a protein domain

locally folded unit of a tertiary structure with a specific function

71
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what does kinase do?

adds phosphotase

72
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what does phosphotase do?

removes phosphate group

73
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cut the py

cytosine, uracil, thymine = pyrimidine

74
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GA the pur

guanine, adenine= purine

75
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what is a nucleoside

a base covalently bonded to sugar with no phosphate group

76
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what direction are 5’ and 3’

antiparallel

77
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where does binding occur?

3’ OH

78
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what is the difference between RNA and DNA nucleotides?

RIBOSE sugar (RNA) and DEOXYRIBOSE sugar (DNA)

79
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what are chromosomes

proteins with a single molecule of DNA

80
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what is a genome?

information contained within the organism’s DNA

81
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what type of DNA has circular chromosomes?

prokaryotic

82
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what is an RNA and DNA hybrid

r loop

83
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what is the process of prokaryotic RNA transcription

binding, initiation, elongation, termination

84
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what does RNA polymerase do?

copies DNA sequence into RNA sequence

85
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what is the promoter

where RNA polymerase first binds

86
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what is the terminator

the end of transcription region

87
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what type of bond holds together beta plated sheets

hydrogen bonds

88
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why are enzymes catalysts of biochemical reactions

they reduce the activation energy of a reaction

89
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where does a competitive inhibitor bind to an enzyme?

active site

90
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what is the +1 site of a gene

where the first nucleotide of RNA is encoded

91
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the enzyme that synthesizes most mRNA in prokaryotes is

RNA polymerase (no number)

92
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the enzyme that synthesizes most mRNA in eukaryotes is

RNA polymerase II