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What are proteins composed of
Amino acids
How many amino acids are used to make proteins
Twenty
What type of bond links amino acids
Peptide bond
What groups form a peptide bond
Carboxyl and amino groups
How many codons encode amino acids
Sixty one
How many stop codons exist
Three
What is meant by degeneracy of the genetic code
Multiple codons encode the same amino acid
Which amino acids have only one codon
Methionine and tryptophan
What codon is used for initiation
AUG
What does mRNA do
Encodes protein sequence
What is the role of rRNA
Forms part of ribosome and catalyses translation
What is the role of tRNA
Brings amino acids and matches codons
What is the structure of tRNA
Cloverleaf
What sequence is added to tRNA after transcription
CCA tail
What unusual bases are found in tRNA
Pseudouridine and dihydrouridine
What is aminoacylation
Charging of tRNA with amino acid
What enzyme carries out aminoacylation
Aminoacyl tRNA synthetase
What cofactor is required for aminoacylation
ATP
What is a charged tRNA
Aminoacyl tRNA
Where is the amino acid attached on tRNA
Three prime or two prime OH of terminal adenine
How many aminoacyl tRNA synthetases exist
At least twenty
What ensures specificity in aminoacylation
Editing by synthetases
What type of base pairing occurs between codon and anticodon
Watson Crick pairing
What is wobble pairing
Flexible pairing at third codon position
What does wobble contribute to
Degeneracy of genetic code
What is usually the first amino acid in proteins
Methionine
What special tRNA is used for initiation in prokaryotes
tRNAfmet
What special tRNA is used for initiation in eukaryotes
tRNAimet
What is used for elongation methionine
tRNAmmet
What are the two ribosomal subunits
Large and small
What molecule makes up most of the ribosome
rRNA
What is the rate limiting step of translation
Initiation
What sequence helps ribosome bind mRNA in prokaryotes
Shine Dalgarno sequence
Where does Shine Dalgarno bind
Sixteen S rRNA
What do IF1 and IF3 do
Guide initiator tRNA and prevent large subunit binding
How many sites are in the ribosome
Three
What are the ribosome sites
A P and E
What is the A site
Aminoacyl site
What is the P site
Peptidyl site
What is the E site
Exit site
What does EFTu do
Brings aminoacyl tRNA to ribosome
What happens to EFTu during elongation
Hydrolyses GTP and leaves
What catalyses peptide bond formation
Peptidyl transferase centre
Is peptidyl transferase a protein enzyme
No
What type of molecule catalyses peptide bond formation
Ribozyme
What ribosomal subunit contains peptidyl transferase
Fifty S subunit
What are ribozymes
Catalytic RNA molecules
What cellular processes involve ribozymes
RNA splicing and intron removal
What is translocation
Movement of ribosome along mRNA
What direction does ribosome move
Three prime direction
What factor is required for translocation
EFG
What energy source is required for translocation
GTP
What happens to peptidyl tRNA during translocation
Moves from A site to P site
What happens to uncharged tRNA during translocation
Moves from P site to E site
What happens to EFG after translocation
Released and reused
What is structural similarity between EFG and EFTu
EFG mimics EFTu tRNA complex
Where does EFG bind
A site
What drives conformational changes during translocation
GTP hydrolysis
How far does ribosome move each step
Three bases
What are the steps of elongation
tRNA binding peptide bond formation and translocation
What happens to tRNA in E site during elongation
It is displaced
How long can polypeptide chains become
Over one thousand amino acids
What happens at stop codons
Release factors bind
What does RF1 recognise
UAA and UAG
What does RF2 recognise
UAA and UGA
Why does no tRNA bind stop codons
No corresponding anticodon exists
What is ribosome recycling factor
Protein that helps disassemble ribosome
What promotes ribosome disassembly
RRF and EFG GTP
What does IF3 do during recycling
Stabilises small subunit