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Biochem exam 3 > Protein Synthesis and Protein Functions > Flashcards

Protein Synthesis and Protein Functions Flashcards

1
Q

What is the process of creating custom treatment based on the genetic basis of condition?

A

precision medicine

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2
Q

What is translation?

A

the process of making a peptide chain using mRNA that is read 5’-3’
-codons are 3 nucleotides in a row that are read by the anticodons on tRNA

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3
Q

which RNA contains all anticodons?

A

tRNA

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4
Q

Where is translation completed?

A

in the ribosomes

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5
Q

What is the structure of ribosomes?

A

2 subunits (40s and 60s)
-33 proteins in the 40s subunit
-46 proteins in the 60s subunit
-there are 4 rRNAs that make up the ribosomes: 18S, 28S, 5.8S, and 5S rRNA

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6
Q

What is the most abundant RNA in the cell?

A

rRNA

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7
Q

How is 18S, 28S, and 5.8S rRNA made?

A

transcribed by RNA polymerase I
-further processed in the nucleolus

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8
Q

How is 5S rRNA made?

A

transcribed by RNA polymerase III outside the nucleolus

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9
Q

What transcribes mRNA?

A

RNA polymerase II

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10
Q

What are the functions of rRNA in the ribosomes?

A
  1. structural- framework that hold ribosomal proteins together
  2. facilitate chemical reactions involved in peptide elongation
  3. binding sites for tRNA
  4. conformational changes- allow ribosome to move along the mRNA
  5. subunit coordination- aid proper alignment of 40S and 60S subunit
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11
Q

What do RNA modifications allow?

A
  1. Ribosome assembly
  2. ribosome stability
  3. tRNA recognition
  4. codon-anticodon interactions
  5. peptide bond formation
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12
Q

What are some possible modifications of rRNA?

A

-methylation of 2-OH position on the nucleotide ribose sugar
-isomerization of uridine nucleotides to pseudouridine
-acetylation

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13
Q

What guides rRNA modification?

A

snoRNA

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14
Q

Where does a majority of ribosome assembly occur?

A

in the nucleolus

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15
Q

What are the two types of ribosomes?

A

membrane bound and free

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16
Q

What are membrane bound ribosomes?

A

the most abundant type
-located on the surface of ER

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17
Q

What are free ribosomes?

A

move anywhere in the cytosol
-make proteins in the cytoplasm

18
Q

Where do proteins made in membrane bound proteins go?

A

exported out of the cell or to the plasma membrane

19
Q

What allows for mRNAs to be translated? (as opposed to other RNAs)

A

the have a poly A tail that allows them to exit the nucleus
-allows for formation of mRNA activation complex

20
Q

What are the two components of the translation initiation complex?

A
  1. mRNA activation complex
  2. pre-initiation complex
    -40s subunit
    -multiple initiation factors
    initiator methionine tRNA
21
Q

What is an anti-codon?

A

three nucleotides that associate with the codon on mRNA through base pairing

22
Q

What allows for a decrease in the number of tRNAs required?

A

redundancy in the genetic code
-inosines in the first position allow for binding of any nucleotide in the third position of codon

23
Q

What are the roles of charged tRNAs?

A

-use anticodons to read codons
-become charged when amino acids bind

24
Q

What are the steps of translation?

A

-initation
-elongation
-terminatioin

25
Q

Process of translation:

A

-first methionine codon in P site
-next aminoacyl-tRNA binds in the A site
-methionine released form tRNA
-peptide bond formed between it and the amino acid on the tRNA in the A site
-ribosomes moves 5’ to 3’ along the mRNA discharging the empty tRNA and shift peptide into the P site
-process is repeated over until a stop codon
-termination of polypeptide chain involves hydrolysis of the ester bond, releasing the protein

26
Q

What is the primary structure of a protein?

A

the amino acid sequence in a chain

27
Q

What is the secondary structure of a protein?

A

stretches of polypeptides that form alpha helices and beta sheets
-held in shape by hydrogen bonds

28
Q

What is the tertiary structure of a protein?

A

refers to the 3D structure of the protein
-formed due to interactions between R groups

29
Q

What is the quaternary structure of a protein?

A

designation for proteins that are made of more than one polypeptide chain
-complete structure of all polypeptides

30
Q

What are motifs of proteins?

A

shared sequences of amino acids that can be used to identify potential members of a protein family

31
Q

What are domains of proteins?

A

structural entities that function independently within a protein and can be built from a specific motif or set of motifs

32
Q

What are examples of protein sequence motifs?

A

-proteolytic enzyme cleavage sites
-phosphorylation sites
-binding motifs
-transmembrane spanning sequences
-protein secretion leader sequences
-transcription factor DNA recognition sequences

33
Q

How do mutations affect protein function?

A

removing or changing amino acids that define a motif or domain can have an affect on secondary, tertiary, and even quaternary structure
-this will affect the way that proteins can function

34
Q

What does amelogenin do?

A

stabilize the amorphous Ca-P phase
-control apatite crystal morphology and organization, control of enamel thickness
-ability to self assemble into nanospheres and guide HAP crystal formation/growth

35
Q

What does ameloblastin do?

A

cell adhesion protein, controls cell differentiation, maintains rod integrity

36
Q

What does enamelin do?

A

cooperates with amelogenin to control mineral nucleation and elongated growth

37
Q

What does Kallikrin 4 do?

A

digests enamel proteins during maturation stage facilitating their removal and hardening the final layer of enamel

38
Q

What does Mmp-20 do?

A

cleaves amelogenin, ameloblastin, and enamelin at the secretory stage to produce stable intermediates with defined functions

39
Q

As apatite crystals grow, what happens to amelogenin?

A

it is removed

40
Q

What is the amelogenin dependent on?

A

hydrophilic C terminal

41
Q

What is the structure of amelogenin?

A

double-ring barrel (six dimers) and assemble into structured nanospheres

42
Q

Mutations in amelogenin cause…

A

amelogenesis imperfecta

Biochem exam 3 (10 decks)

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