Biology Translation Overview

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Questions and Answers

Which structural class of proteins provides support to the cell?

  • Structural proteins (correct)
  • Enzymes
  • Transport proteins
  • Signal proteins

What type of reaction forms a peptide bond?

  • Dehydrogenation reaction
  • Dehydration reaction (correct)
  • Condensation reaction
  • Hydrolysis reaction

Which of the following amino acids is classified as basic?

  • Histidine (correct)
  • Phenylalanine
  • Aspartic Acid
  • Tyrosine

Which statement best describes the primary structure of proteins?

<p>It is a linear sequence of amino acids linked by peptide bonds. (D)</p> Signup and view all the answers

Which part of an amino acid varies among different amino acids?

<p>Radical group (side chain) (A)</p> Signup and view all the answers

What is the primary function of enzymes?

<p>Act as biological catalysts (D)</p> Signup and view all the answers

What does the term 'tertiary structure' in proteins refer to?

<p>The 3D shape formed by side chain interactions (B)</p> Signup and view all the answers

Which of the following amino acids is nonpolar?

<p>Leucine (B)</p> Signup and view all the answers

What type of bond primarily stabilizes the triple helix structure of collagen?

<p>Hydrogen bonds (C)</p> Signup and view all the answers

Which of the following statements about the secondary structure of an alpha helix is true?

<p>Hydrogen bonds form between the oxygen of one turn and the hydrogen of another turn. (A)</p> Signup and view all the answers

What is the primary interaction that leads to the formation of the tertiary structure in proteins?

<p>Interactions between amino acid R groups (C)</p> Signup and view all the answers

Which protein structure involves the assembly of multiple polypeptide chains?

<p>Quaternary structure (B)</p> Signup and view all the answers

What stabilizes the quaternary structure of hemoglobin?

<p>Hydrogen bonds and ionic interactions (D)</p> Signup and view all the answers

Which of the following describes the beta-pleated sheet secondary structure?

<p>It arises from hydrogen bonding between carbonyl oxygen atoms and hydrogen in amide groups. (D)</p> Signup and view all the answers

Which type of interactions are responsible for the folding of a protein into its tertiary structure?

<p>Hydrophobic interactions and molecular interactions (A)</p> Signup and view all the answers

How many polypeptide chains are typically found in a hemoglobin molecule?

<p>Four (A)</p> Signup and view all the answers

What dictates the correct reading frame in mRNA translation?

<p>The start codon (A)</p> Signup and view all the answers

How many different reading frames can a single mRNA sequence have?

<p>Three (B)</p> Signup and view all the answers

What happens when the ribosome encounters a start codon?

<p>It begins reading the mRNA in codons (D)</p> Signup and view all the answers

Which sites are present on the large subunit of a ribosome?

<p>P, A, E (B)</p> Signup and view all the answers

What is the main function of the anticodon in tRNA?

<p>To bind with the correct codon on mRNA (D)</p> Signup and view all the answers

What is the role of the wobble position in codon-anticodon pairing?

<p>Facilitates non-Watson-Crick base pairing (C)</p> Signup and view all the answers

What type of structure does tRNA have that is crucial for its function?

<p>Minimum of three stem loop structures (B)</p> Signup and view all the answers

Which of the following components is NOT part of the translation process as described?

<p>DNA polymerase (D)</p> Signup and view all the answers

What is the first step in the initiation of translation for prokaryotes?

<p>Association of the small subunit with the Shine Delgarno sequence (C)</p> Signup and view all the answers

What role does GTP play during the initiation phase of translation in prokaryotes?

<p>It triggers binding of the large subunit to the small subunit (A)</p> Signup and view all the answers

What is the primary role of hemoglobin in the body?

<p>Capture and delivery of oxygen (B)</p> Signup and view all the answers

How do ribosomes recognize which amino acids to use during translation?

<p>Through a sequence of codons specified by mRNA (B)</p> Signup and view all the answers

During which phase of translation is the polypeptide chain created?

<p>Elongation (D)</p> Signup and view all the answers

What occurs when proteins misfold or mutate?

<p>They can cause cellular damage (A)</p> Signup and view all the answers

Which phase of translation requires charged tRNAs and elongation factors?

<p>Elongation (A)</p> Signup and view all the answers

What occurs during the translocation step of elongation?

<p>The ribosome moves to read the next codon (A)</p> Signup and view all the answers

Which of the following codons acts as a start signal for translation?

<p>AUG (B)</p> Signup and view all the answers

What is the genetic code considered to be?

<p>Degenerate with multiple codons for some amino acids (A)</p> Signup and view all the answers

What is the role of initiation factor 3 (IF-3) during translation initiation?

<p>To prevent large and small subunits from binding (A)</p> Signup and view all the answers

In which site of the ribosome does the charged tRNA enter during elongation?

<p>A site (D)</p> Signup and view all the answers

Which of the following accurately describes the structure of a ribosome?

<p>Made up of protein and rRNA with two interacting subunits (A)</p> Signup and view all the answers

Why is the quaternary structure of a protein important?

<p>It dictates how the protein interacts with other molecules (B)</p> Signup and view all the answers

What happens to the tRNA located in the P site after a peptide bond forms?

<p>It releases its amino acid (D)</p> Signup and view all the answers

What is the role of tRNA in protein synthesis?

<p>To carry specific amino acids to the ribosome (D)</p> Signup and view all the answers

Flashcards

Central Dogma of Molecular Biology

DNA is transcribed into RNA, which is then translated into protein.

Protein Structure: Primary

The linear sequence of amino acids linked by peptide bonds.

Protein Structure: Secondary

Folding of the polypeptide chain due to hydrogen bonds between amino acid backbones, forming alpha helices and beta-pleated sheets.

Amino Acid

Building block of proteins; composed of an amino group, a carboxyl group, a hydrogen, and a variable side chain (radical group).

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Peptide Bond

Covalent bond formed between two amino acids through a dehydration reaction.

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Structural Protein

Proteins that provide support and shape to cells.

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Enzyme

Biological catalysts that speed up chemical reactions.

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Protein Structure: Tertiary

Three-dimensional folding of a polypeptide chain due to interactions between side chains (R-groups).

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Quaternary Structure

The arrangement of multiple protein subunits, stabilized by interactions like those in tertiary structure.

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Alpha Helix

A spiral-shaped secondary protein structure, stabilized by hydrogen bonds.

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Beta-Pleated Sheet

A sheet-like secondary protein structure, stabilized by hydrogen bonds.

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Triple Helix

Three polypeptide chains intertwined, stabilized by hydrogen bonds.

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Tertiary Structure

The 3D shape of a protein, formed by interactions between amino acid R-groups.

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Hemoglobin

A protein in red blood cells that carries oxygen.

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Disulfide Bonds

Strong covalent bonds between cysteine amino acids.

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Protein Subunits

Individual protein chains that combine to form a larger protein.

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Protein Structure & Function

Protein's shape dictates its job. Changes in structure can significantly affect its function. Misfolded proteins can cause cellular damage, and some are even harmful (prions).

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Ribosomes

Cellular structures that build proteins by reading mRNA's instructions.

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tRNA

RNA molecules that carry specific amino acids to the ribosome during protein synthesis.

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mRNA

Instructions for protein synthesis read by ribosomes; determines which amino acids to use.

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Codon

A three-nucleotide sequence on mRNA that codes for a particular amino acid.

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Genetic Code

Universal set of rules that dictates which codons correspond to which amino acids.

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Start Codon (AUG)

Codon that signals the start of protein synthesis, specifies methionine.

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Stop Codons (UAG, UAA, UGA)

Codons that signal the end of protein synthesis.

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Reading frame

The way a sequence of mRNA is divided into codons, influencing the polypeptide produced.

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Start codon

The first codon in an mRNA sequence that initiates translation, typically AUG.

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Anticodon

A sequence of three nucleotides on tRNA that base-pairs with a complementary codon on mRNA.

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Wobble hypothesis

Explains how a single tRNA can recognize multiple codons due to flexibility in the third base pairing.

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What are the three tRNA binding sites on the ribosome?

The ribosome has three tRNA binding sites: the A site (aminoacyl) for incoming tRNA, the P site (peptidyl) for the tRNA holding the growing polypeptide, and the E site (exit) for the departing tRNA.

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How is the polypeptide chain built?

Amino acids brought by tRNA molecules are added to the growing polypeptide chain through peptide bond formation, driven by the ribosome.

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Translation

The process of converting genetic information from mRNA into a protein polypeptide chain. It involves three steps: initiation, elongation, and termination.

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Initiation of Translation

The first step of translation, where the ribosome assembles on the mRNA, setting the stage for protein synthesis.

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Shine-Dalgarno Sequence

A specific sequence in mRNA (5' UAAGGAGGU 3') recognized by the small ribosomal subunit in prokaryotes, guiding ribosome binding to the mRNA

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Elongation in Translation

The second step of translation, where the polypeptide chain is created as the ribosome moves along the mRNA, adding amino acids.

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Translocation in Translation

The process in elongation where the ribosome shifts one codon forward on the mRNA, moving the tRNA carrying the growing polypeptide from the A site to the P site.

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Termination of Translation

The final step of translation where the ribosome detaches from the mRNA and the newly synthesized polypeptide is released.

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Charged tRNA

A tRNA molecule that carries an amino acid attached to its acceptor stem, ready to be incorporated into a growing polypeptide chain.

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tRNA Anticodon

A three-nucleotide sequence on a tRNA that recognizes and base pairs with a complementary codon on mRNA, ensuring the correct amino acid is added to the growing polypeptide.

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Study Notes

Translation Overview

  • Translation is the process of converting mRNA into a protein.
  • It involves the machinery of the ribosome and transfer RNA (tRNA).

Central Dogma Analogy

  • The process is analogous to a cookbook (DNA), instructions (mRNA), and final product (protein/cookie).
  • The analogy shows how DNA codes for mRNA, and how mRNA codes for protein.

mRNA and Proteins

  • mRNA is translated into proteins.
  • Proteins are composed of amino acids.
  • There are 20 different amino acids.

Amino Acids

  • Each amino acid has unique properties (size, charge, etc.).
  • Amino acids are linked together by peptide bonds.
  • The product formed is called a polypeptide.

General Structure of Amino Acid

  • An amino acid has an amino group (+H3N), carboxyl group (COO-), a central carbon atom (α-carbon), and a radical group (R-group/side chain).

Amino Acid Classification

  • Amino acids can be classified into nonpolar, polar, and charged groups.

Peptide Bond Formation

  • Peptide bonds are formed via a dehydration reaction.
  • This reaction removes a water molecule.

Protein Structure Levels

  • Proteins have four levels of structure: primary, secondary, tertiary, and quaternary.

Primary Structure

  • Linear sequence of amino acids.
  • Amino acids are linked by peptide bonds.

Secondary Structure

  • Hydrogen bonding between amino acid backbones causes alpha helices and beta-pleated sheets.
  • An alpha helix is like a spiral staircase.
  • A beta-pleated sheet is like folded paper.

Secondary Structure: Triple Helix

  • Three polypeptide chains are intertwined by hydrogen bonds to form a triple helix.
  • Often found in collagen.

Tertiary Structure

  • Interactions among side chains (R groups) fold the protein into a three-dimensional shape:
    • Hydrophobic interactions between nonpolar amino acids.
    • Hydrophilic interactions between polar amino acids and water.
    • Salt bridges between ionized R groups of basic and acidic amino acids.
    • Hydrogen bonds between polar R groups.
    • Disulfide bonds between cysteine amino acids.

Quaternary Structure

  • Multiple polypeptide chains interact to form a functional protein complex.
  • Hemoglobin, made up of four polypeptide chains, is an example.

Protein Structure and Function

  • The specific shape of a protein directly influences its function.
  • Even small changes in the protein's structure can have a significant impact on its activity.
  • Prions are misfolded proteins that cause other proteins to adopt their abnormal conformation, leading to disease.

Translation Machinery

  • Ribosomes are the sites of protein synthesis.
  • They have two subunits (large and small).
  • Transfer RNAs (tRNAs) carry specific amino acids to the ribosome to match to mRNA's codons.

Universal Genetic Code

  • mRNA uses codons (three nucleotides) to specify amino acids.
  • The genetic code is universal, which means the same codons specify the same amino acids in all organisms.
  • It contains 64 codons, but only 20 amino acids.
  • Many codons specify the same amino acid.

Codon Recognition

  • The anticodon on a tRNA molecule binds with the codon on the mRNA.
  • This ensures the correct amino acid is added to the growing polypeptide chain.

Wobble Hypothesis

  • The third base of a codon can sometimes tolerate variations in base pairings.
  • This allows a single tRNA to recognize multiple codons, accounting for why the genetic code is redundant.
  • The wobble position is a beneficial feature that ensures accuracy in amino acid incorporation.

Translation Steps: Initiation

  • Ribosome assembles on mRNA.
  • Initiation factors help assemble the ribosome.
  • The ribosome's small subunit binds to the mRNA’s Shine-Dalgarno sequence.
  • The first tRNA (carrying methionine) binds to the mRNA's Start codon (AUG). -This tRNA fits into the ribosome's P site.

Translation Steps: Elongation

  • Charged tRNAs in the complex, with the help of elongation factors, bind to the A site.
  • A peptide bond forms between the amino acids in the A and P sites.
  • Translocation occurs: the ribosome moves to the next codon.
  • The tRNA in the P site moves to the E site (exits). The tRNA in the A site moves to the P site.

Translation Steps: Termination

  • The ribosome encounters a stop codon (UAG, UAA, or UGA).
  • Release factors (RFs) bind to the A site instead of a tRNA.
  • The polypeptide chain is released.
  • The ribosome disassembles.

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