Molecular Biology - Functions of Macromolecules

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Last updated 7:39 PM on 8/15/26
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131 Terms

1
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Define the unified cell theory.

1. The cell is the most basic unit of life. 2. All living things are made up of ≥ cell. 3. New cells are made from existing cells.

2
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Name the properties of life

Order/Hierarchy of molecule interactions, Energy processing and general catalysis, Both responsive to (stimuli) and resistant to (homeostasis) environment, reproduction, growth and development directed by a genetic material, regulation of metabolism and material transfer (plasma membranes), adaptation (in individuals) and Evolution (of populations over time)

3
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Name the monomer, polymer and bond of carbohydrates:

monosaccharides, disaccharide/polysaccharide, glycosidic

4
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Name the monomer, polymer and bond of proteins:

amino acids, polypeptide, peptide

5
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Name the monomer, polymer and bonds of nucleic acids:

nucleotides, oligonucleotides/polynucleotides, phosphodiester

6
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Name the monomer, polymer and bond of lipids:

fatty acids + glycerol/sphingosine, triacylglycerol, phospholipids, ester

7
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From purely structural perspective: Sugars are used to build ___ of the 4 macromolecules.

3

8
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_____ can decorate proteins to create signals, or the ____ can be the signal in itself.

Sugar

9
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______ is a glycoprotein hormone that stimulates RBC production.

Erythropoietin

10
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GlcNAc presence is indicative of cellular _____ stores.

energy

11
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What is a chain of amino acids in protein structure?

primary structure

12
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What is the local folding of the polypeptide chain connected by Hydrogen bonds and include α-helices, and β-strands/sheets and turns?

secondary structure

13
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What is the folding of the secondary structure, connected by disulfide linkages and commonly observed sections of tertiary structure called motifs?

tertiary structure

14
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What is the interaction of multiple peptides?

quaternary structure

15
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What is the role of amylase, polymerases, ligases that help with catalysis and make chemical reactions go faster?

enzyme

16
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What is the role of hemoglobin, albumin and carry substances throughout an organism?

transport

17
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What is the role of actin, tubulin, and keratin that construct rigid structures within cells/organs?

Structure

18
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What is the role of insulin, thyroxin, and are chemical signal molecules?

hormones

19
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What is the role of immunoglobulins and function to protect the organism from pathogens?

defense

20
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What is the role of actin, myosin that effect contraction of cellular structure?

motion

21
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What is the role of albumin that are a food source for embryonic organisms?

storage

22
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What is the role of chaperone proteins that help other proteins to fold correctly?

folding

23
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Activators _____ moving forward.

promote

24
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Inhibitors _____ stop forward progress.

prevent

25
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Substrate- level control acts on a ______ step in a pathway.

single

26
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Feedback control targets a _____ step in a pathway.

different

27
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What is the regulation of protein function in an on/off fashion in synthesis vs degradation and all pieces in the proper location

availability

28
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What is the regulation of protein function like a volume dial in adding or subtracting pieces, extra molecules may be required and protein families consist of similar yet distinct proteins?

Activity

29
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____ ____ is a multi-step process that only occurs at certain times in a cell's lifecycle.

Gene expression

30
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Proteins are _____ when they are deemed undesirable or unnecessary.

degraded

31
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Eukaryotes have many compartments, and chemical reactions only occur in certain places in the cell. This regulatory strategy is called _______

compartmentalization

32
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The transmission of ____ ____ , e.g. substrates or ligands, starts with an external cue

signaling molecules

33
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___ ____ are reversible +/- ≥ 1 \"functional groups\" to activate/inactivate the enzyme.

covalent modifications

34
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Name 8 covalent modifications:

phosphorylation, acetylation, myristoylation, ADP ribosylation, farnesylation, γ- Carboxylation, sulfation, ubiquitination

35
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Name common additions in the reversible covalent modifications:

lipids, nucleic acids, proteins, carbohydrates, small molecules

36
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What common addition are myristoylate and farnesyl?

lipid

37
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What common addition are ADP-ribose?

nucleic acids

38
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What common addition are blood typing, M6P sorting signal?

carbohydrates

39
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What common addition is ubiquitin?

proteins

40
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What common addition are phosphate, sulfate, acetyl, and methyl?

small molecules

41
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What adds phosphates?

kinases

42
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What removes phosphates?

phosphatases

43
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Phosphates can be activating or ______.

inhibiting

44
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Name the irreversible covalent modification:

the case of proteolytic activation

45
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What are the enzymes that are digestive enzymes, collagenase (development), and caspases (apoptosis) considered?

proteases

46
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What enzymes/proteins need to be cut apart in order to be fully activated?

Proteases, Collagen, Blood Clotting Factors, Insulin/Hormones

47
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What is an effector (activator or inhibitor) molecule that alters substrate binding?

Heteroallostery

48
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The ____ site is where the chemical reaction takes place or work is performed?

active

49
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The _____ site is a different location on the enzyme where an effector binds or regulation occurs.

allosteric

50
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____ = cooperativity: each substrate binding alters subsequent substrate binding efficiency.

homoallostery

51
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In _____ cooperativity, the next substrate has an easier time binding/better binding. In _____ cooperativity, the next substrate has a more difficult time binding/worse binding.

positive, negative

52
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What help in regulation of enzyme activity with metal ions/inorganic?

cofactors

53
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What help in regulation of enzyme activity with vitamins and other macromolecule derivatives/organic?

coenzymes

54
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Protein quaternary structure varies based on the available _____ also called isoforms.

isozymes

55
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Isozymes catalyze the ____ reaction but with _____ efficiencies.

same, different

56
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Name the mix and match subunits of enzyme activity:

heterozygous alleles, homologs (paralogs/gene duplications/evolutionary relations), alternative splicing, monomer vs dimer/trimer/etc., +/- covalent modifications, conformations.

57
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_______ isozymes result in tissue specificity

compartmentalized

58
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_____ expression of isozymes is common in development

temporal

59
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___ _____ participates in the lactic acid fermentation pathway, is a tetramer, and isoforms say where they are expressed in the heart or skeletal muscle.

lactate dehydrogenase LDH

60
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Cells contain two types of nucleic acids:

DNA, RNA

61
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What is the function of DNA?

storage of information

62
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What is the function of RNA?

transport, catalysis, regulation

63
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What is the structure of DNA?

2 strands

64
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What is the structure of RNA?

1 strand

65
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What is the sugar of DNA?

deoxyribose

66
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What is the sugar of RNA?

ribose

67
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What are the pyrimidines of DNA?

C,T

68
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What are the pyrimidines of RNA?

C,U

69
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What are the purines of DNA?

A,G

70
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What are the purines of RNA?

A,G

71
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What are the three parts of nucleotides?

(Deoxy)ribose sugar, A phosphate group, Nitrogenous Base

72
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In DNA the carbons on the sugar are numbered _____ and nucleotides are linked through the phosphate _______ bond to create a chain that runs ____

1'-5', phosphodiester, 5'-3'

73
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What are the four nitrogenous bases of DNA?

The Purines: adenine, guanine, and pyrimidines: Thymine, Cytosine

74
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How many rings do purines have?

2

75
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How many rings do pyrimidines have?

1

76
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Purines always base-pair with _____ creating an ______ double helix of consistent width.

pyrimidines, antiparallel

77
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The ____ ___ ____ states that the cell is the most basic unit of life, all living things are made up of ≥ cell, new cells are made from existing cells.

Unified Cell Theory

78
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Cells must contain a ____ ____ that is passed from one generation to the next and directs the creation of the next generation.

genetic material

79
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What are the 4 characteristics of genetic material?

replication of self, stable storage of information, expression of information, variation through mutation

80
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Explain the transformation experiment done by Frederick Griffith

injects living IIIS virulent mouse dies, injects living IIR avirulent mouse lives, injects heat-killed IIIS mouse lives, mixes heat-killed IIIS and living IIR avirulent mouse dies living IIIS recovered

81
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Who did transformation experiments to confirm active factor was DNA?

Frederick Griffith, Oswald Avery, Colin MacLeod, and Maclyn McCarty

82
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Who did bacteriophage confirmation?

Alfred Hershey and Martha Chase

83
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Genetic material is both _____ and ______ to sustain life.

necessary, sufficient

84
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The Central Dogma of Molecular Biology states if DNA is the genetic material, then it must:

1. Template its own replication, 2. Encode the expression of proteins through an RNA intermediate

85
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Nucleoside Triphosphates can be used for:

Making more DNA/RNA, Providing energy ATP and GTP, and Regulating cellular functions GTP

86
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_____ is the regulatory nucleotide.

GTP

87
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G proteins are GTPases: They _____ GTP or removal a phosphate.

hydrolyze

88
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_____ regenerate G proteins by replacing spent GDP with fresh GTP.

GEFs or Guanine nucleotide Exchange Factors

89
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_____ stimulate G proteins to hydrolyze GTP, thereby inactivating the enzyme.

GAPs or GTPase-Activating Proteins

90
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What is the location of carbohydrates in the cell?

storage/vacuole decorating lipids and proteins

91
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Where is the location of proteins in the cell?

everywhere

92
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Where is the location of nucleic acids in the cell?

nucleus, mitochondria, chloroplasts, cytosol

93
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Where is the location of lipids in the cell?

membranes

94
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What macromolecule's role is molecule identification, protection, and energy production?

carbohydrates

95
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What macromolecule's role is to perform work?

proteins

96
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What macromolecule's role is genetic material, energy, and regulation?

nucleic acids

97
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What macromolecule's role is semi-permeable and membranes?

lipids

98
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What macromolecule is rigid, sticky/slimy?

carbohydrates

99
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What macromolecule is fibers and globules?

proteins

100
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What macromolecule is viscous and snotty?

nucleic acids