Exam 2 + 3 Material Flashcards

1
Q

Genetic Code

A
  • Some codons do not encode any amino acid
  • The initiation codon establishes the reading frame for ribosomes
  • Every possible codon has some function in translation
  • Methionine is only encoded by one codon
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2
Q

What is false about genetic code

A
  • All amino acids are encoded by more than one codon
  • WRONG because most are but all are not
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3
Q

Aminoacyl-tRNA Synthetase functions

A
  • Attachment of amino acid to AMP
  • Attachment of amino acid to tRNA
  • Proofreading correct amino acid-tRNA linkage
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4
Q

Ubiquitylation

A
  • Targets a protein for degradation
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5
Q

Random coils

A

Flexible regions that link secondary structures together

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6
Q

What steps of protein synthesis that requires ATP hydrolysis

A

Attachment of amino acid to tRNA

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7
Q

What steps of protein synthesis that require GTP hydrolysis

A
  • Translocation of a ribosome from one codon to another
  • Proofreading anticodon-codon pairing
  • Binding a release factor to a stop codon
  • Ef-Tu
  • eIF2
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8
Q

Kd value

A
  • Lower Kd = strong binding
  • High Kd = weak binding
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9
Q

Function of phosphorylation as a post-translational modification

A
  • Adds a negative charge to a protein
  • Generates a binding site for proteins containing an SH2 domain
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10
Q

How can antibiotics selectively affect prokaryotic cells and why are there side effects on eukaryotic cells

A
  • Affect prokaryotes due to differences in ribosomes
  • There are side effects because organelles such as the mitochondria and chloroplasts have similar ribosomes to prokaryotes
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11
Q

Where does proofreading occur in protein synthesis

A

When aminoacyl-tRNA synthetase checks for codon-anticodon pairings to prevent mistakes during protein synthesis

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12
Q

Domains

A
  • Independent folding regions within a protein that contains different functions
  • The tertiary structure of proteins contains different domains
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13
Q

Post-transcriptional modifications

A
  • Addition of 7-methylguanosine cap to the 5’ end of RNA
  • mRNA splicing
  • Formation of 3’ end poly-A tail
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14
Q

Advantage of the addition of a 7-methylguanosine cap to the 5’ end of RNA

A

This signals that this is an mRNA to be and the 5’ end is intact

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15
Q

Advantage of mRNA splicing

A
  • Splicesome removes introns from the codon sequence
  • This allows for a diversified production of proteins through alternative splicing
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16
Q

Advantage of 3’ end poly-A tail

A
  • The original 3’ end of RNA is cleaved off
  • About 200 A’s are added to the 3’ end via poly-A polymerase
  • This signals that the RNA is now mature and can be exported to the cytoplasm for translation
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17
Q

Introns

A
  • Non-coding sequences
  • Interrupts actual coding sequence
  • However: They allow many different variations of proteins through alternative splicing
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18
Q

Features of 5’ cap on pre-mRNA

A
  • Has 5’ to 7’ methylguanosine
  • It is 5’ to 5’
  • Has a triphosphate linkage
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19
Q

Outer mitochondrial membrane

A

Contains porins that exchange material between the cytoplasm and mitochondria

20
Q

Inner mitochondrial membrane

A
  • Cardiolipin
  • Cristae: site of ETC and provides SA
21
Q

Mitochondrial Intermembrane space

A
  • Cytochrome C
  • Factors that program cell death
22
Q

Mitochondrial matrix

A
  • Site of oxidative metabolism
  • Contains mDNA and ribosomes
23
Q

Enzyme Catalysis

A
  • Decrease the activation energy for a chemical reaction
  • Increase the rate of forward and reverse reactions
24
Q

What can enzymes NOT do

A
  • Do not alter delta G
  • No effect on net equilibrium
  • No effect on reactant and product concentrations
  • Cannot make a reaction occur spontaneously
25
Q

Irreversible inhibitors

A
  • Covalently bind to amino acid residues
  • Cannot be overcome by increasing substrate concentration
  • Inactive and remove active enzymes
  • Lower Vmax
26
Q

Reversible Inhibitors

A
  • Competitive
  • Non-competitive
27
Q

Non-competitive inhibitor

A
  • Reduces Vmax
  • No effect on Km
  • Bind away from the active site
28
Q

Competitive inhibitor

A
  • Increase Km
  • No effect on Vmax
  • Compete with the substrate to bind to the active site
29
Q

DNA binding motifs WITH a dimerization region

A
  • Leucine zipper
  • Helix-loop-helix
  • Second class of zinc fingers
30
Q

DNA binding motifs WITHOUT a dimerization region

A
  • Helix-turn-helix
  • Homeodomain
  • First class of zinc fingers
31
Q

Homeodomain characteristics

A
  • Contains 3 alpha helices
  • Similar to helix-turn-helix
  • In contact with major and minor groove of DNA
32
Q

Advantages of cell surface receptors using second messengers

A
  • Signal does not have to travel through the membrane
  • Difficult signaling pathways can occur from the same signal
33
Q

Examples of second messengers

34
Q

What does a homeobox domain contain

A

Helix-turn-helix region

35
Q

How can complexes be organized to increase the speed and efficiency of signaling

A
  • Complexes can be organized into scaffolds
  • Scaffold proteins bind to a cell surface receptor
  • Intracellular signaling molecules bind to the scaffold protein
  • When a signaling molecule is bound to a cell surface receptor, the signaling complex is activated
  • The scaffold sends the signal downstream and further amplifies it
  • Receptor activation can be used
  • Once a receptor is turned on, intracellular signaling proteins can assemble near the receptor which can result in downstream signaling occur
36
Q

Advantage of second messengers

A

Amplifies the signal

37
Q

Types of RNA

A
  • tRNA: responsible for bringing amino acids to ribosomes for translation
  • snRNA: makes up the splicesome and is responsible for splicing RNA
38
Q

Promoters

A
  • Found upstream of DNA
  • Bind to RNA polymerase and initiation complexes
  • Start transcription through binding of TF
39
Q

Enhancers

A
  • Found anywhere on DNA
  • Do not bind to RNA polymerase or initiation complexes
  • Enhance transcription through binding of TF
40
Q

Allosteric regulation

A
  • Allosteric regulators bind away from the catalytic site of an enzyme to a regulatory site
  • This causes a conformational change at the catalytic site which can act as an activator or inhibitor for substrates binding to proteins
  • Can be competitive or non-competitive
41
Q

How can enzymes stabilize the transition state of a chemical reaction

A

When 2 substrates bind to the enzyme, it can orient them in a way that encourages a favorable reaction to occur between them

42
Q

Primary structure

A

Chain of amino acids

43
Q

Secondary structure

A
  • Folding and twisting of the peptide backbone
  • Held together by weak hydrogen bonding between carbonyl and amine groups
  • Contain alpha helices and beta sheets
  • Alpha helices: held together by weak hydrogen bonding between carbonyl and amine groups every 4 amino acids
  • Beta sheets: held together by weak hydrogen bonding between amine and carbonyl groups on adjacent polypeptide chains (run parallel and antiparallel)
44
Q

Tertiary structure

A
  • 3D arrangement of secondary structure
  • Results from noncovalent interactions between R groups or R groups and their environments
45
Q

Quaternary Structure

A
  • Arrangement of multiple tertiary structures
  • Held together by weak bonds and disulfide bonds