CH 13: Translation of mRNA
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These flashcards cover key vocabulary and concepts related to the translation of mRNA and protein structure.
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43 Terms
Methionine
An amino acid that is the only start codon, coded by AUG.
Wobble
A phenomenon where one tRNA can recognize more than one codon.
Polypeptide
A single chain of amino acids held together by peptide bonds.
Primary structure
The order of amino acids in a polypeptide chain determining its folding.
Secondary structure
Unique structures formed in proteins due to hydrogen bonding between amino acids.
Tertiary structure
The overall 3D structure of a protein determined by interactions between amino acids.
Quaternary structure
The arrangement and interaction of multiple polypeptide chains.
Dimer
A protein structure consisting of two polypeptide chains.
Cysteine
An amino acid with a side chain that can form disulfide bonds.
Hydrophobic
Refers to non-polar amino acids that are typically buried within the protein structure.
Polar amino acids
Amino acids that are hydrophilic and likely to be on the surface of proteins.
Histidine
An amino acid that can be phosphorylated and is often targeted by prokaryotic kinases.
Amino acids
Building blocks of proteins, each having a unique side chain (R group).
Stop codon
Codons that terminate translation, including UAG, UAA, and UGA.
Anticodon
A sequence of three nucleotides in tRNA that is complementary to the codon in mRNA.
Protein kinase
An enzyme that adds a phosphate group to specific amino acids in proteins.
Peptide bond
The covalent bond formed between amino acids in a protein.
C terminus
The end of a polypeptide chain that has a free carboxyl group.
Methionine
An amino acid that is the only start codon, coded by AUG.
Wobble
A phenomenon where one tRNA can recognize more than one codon.
Polypeptide
A single chain of amino acids held together by peptide bonds.
Primary structure
The order of amino acids in a polypeptide chain determining its folding.
Secondary structure
Unique structures formed in proteins due to hydrogen bonding between amino acids.
Tertiary structure
The overall 3D structure of a protein determined by interactions between amino acids.
Quaternary structure
The arrangement and interaction of multiple polypeptide chains.
Dimer
A protein structure consisting of two polypeptide chains.
Cysteine
An amino acid with a side chain that can form disulfide bonds.
Hydrophobic
Refers to non-polar amino acids that are typically buried within the protein structure.
Polar amino acids
Amino acids that are hydrophilic and likely to be on the surface of proteins.
Histidine
An amino acid that can be phosphorylated and is often targeted by prokaryotic kinases.
Amino acids
Building blocks of proteins, each having a unique side chain (R group).
Stop codon
Codons that terminate translation, including UAG, UAA, and UGA.
Anticodon
A sequence of three nucleotides in tRNA that is complementary to the codon in mRNA.
Protein kinase
An enzyme that adds a phosphate group to specific amino acids in proteins.
Peptide bond
The covalent bond formed between amino acids in a protein.
C terminus
The end of a polypeptide chain that has a free carboxyl group.
N-terminus
The end of a polypeptide chain that has a free amino group.
Alpha-helix
A common protein secondary structure characterized by a tightly coiled spiral shape stabilized by hydrogen bonds.
Beta-sheet
A common protein secondary structure formed by extended polypeptide strands arranged side-by-side, stabilized by hydrogen bonds, creating a pleated appearance.
Disulfide bond
A strong covalent bond formed between two cysteine residues, critical for stabilizing tertiary and quaternary protein structures.
Molecular chaperone
Proteins that assist in the proper folding of newly synthesized or denatured proteins, preventing aggregation.
Post-translational modification
Covalent modifications to proteins after their synthesis, such as phosphorylation or glycosylation, which can alter function or stability.
Hydrophilic
Refers to polar or charged amino