Questions and Answers
The unfolding of a protein by heat or chemical treatment is referred to as:
The fully folded structure of a functional protein composed of a single polypeptide chain is referred to as:
Proteins that prevent inappropriate folding of newly synthesized proteins are called:
Most proteins retain metabolic activity when denatured.
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Which factor would have an effect on the shape of a protein?
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Which of the following is the actual event that translates the language of nucleic acids to the language of proteins?
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How is the amino acid held on the charged tRNA?
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How many aminoacyl-tRNA synthetase enzymes must be present in cells to properly synthesize proteins?
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The ribosome ______ subunit has ______ binding sites for tRNA molecules.
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Enzymatic catalysis of the peptide bond between the growing polypeptide and the next incoming amino acid takes place in which binding site?
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What feature or structure indicates that this is eukaryotic translation?
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Which of the answer choices occurs in the E site of the ribosome during translation?
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Which step occurs in the P site of the ribosome during translation?
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Which step occurs in the A site of the ribosome during translation?
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When a charged tRNA is about to bind to the vacant A site of a ribosome, where is the growing polypeptide?
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Binding sites for tRNA are located in:
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Assuming A-U and G-C pairing between the anticodon and the codon, what anticodon in tRNAMet would pair with the codon 5′-AUG-3′?
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Ribosomes in prokaryotes and eukaryotes are:
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In a protein-coding region of DNA, any mutation that replaces a single nucleotide for another will replace any amino acid with any other amino acid.
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Protein families contain proteins with identical primary, secondary, and tertiary structures.
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In a population of organisms, beneficial and harmful random mutations are retained or eliminated through the process of:
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An area of a polypeptide that bends in a particular way, relatively independent of the rest of the molecule, is a folding:
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Study Notes
Protein Structure and Translation
- Denaturation is the process where proteins unfold due to heat or chemical treatment, leading to loss of function.
- The fully folded and functional structure of a protein consisting of a single polypeptide chain is termed tertiary structure.
- Chaperones are proteins that assist in the proper folding of newly synthesized proteins, preventing misfolding.
- Most proteins lose metabolic activity upon denaturation; thus, denaturation is typically irreversible and damaging.
- Protein shape is influenced by environmental factors, including hydrophilicity/hydrophobicity of surrounding molecules, pH, ion concentrations, and temperature.
- Aminoacyl tRNA synthetase attaches the appropriate amino acid to tRNA, translating nucleic acid sequences into protein-building blocks.
- The bond holding the amino acid to charged tRNA is a covalent bond, ensuring stable attachment.
- There are 20 different aminoacyl-tRNA synthetase enzymes in cells, each specific to one amino acid.
- The large ribosomal subunit contains three binding sites (A, P, E) for tRNA during translation.
- Enzymatic catalysis of peptide bond formation occurs at the A site within the ribosome.
- In eukaryotic translation, the small ribosomal subunit scans the 5' end of mRNA to find the start codon (AUG).
- During translation, uncharged tRNA is ejected from the E site of the ribosome as it moves to the next codon.
- The P site holds the tRNA with the growing polypeptide chain while the ribosome advances.
- The A site is where an incoming charged tRNA binds, signaling the next amino acid addition.
- When a charged tRNA approaches the vacant A site, the growing polypeptide is located in the P site.
- tRNA binding sites are specifically located within the large ribosomal subunit.
- The anticodon for tRNA^Met that pairs with the codon 5′-AUG-3′ is 5′-CAU-3′, ensuring correct translation via complimentary base pairing.
- Ribosomes in prokaryotes and eukaryotes are structurally similar and utilize the same genetic code for translation.
- Mutations that replace a single nucleotide in a protein-coding region of DNA do not guarantee the replacement of one amino acid with another.
- Protein families do not consist of proteins with identical structures; they can vary while sharing similar functions or sequences.
- Selection in populations determines the retention or elimination of beneficial or harmful mutations.
- A folding domain refers to a specific area of a polypeptide that bends in a specific manner, functioning somewhat independently of the overall molecule structure.
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Test your knowledge of protein structure and translation with these flashcards. Each card presents a term related to protein folding and composition, along with its definition. Perfect for students looking to deepen their understanding of biochemistry.
