Lodish Ch 3: Protein Structure and Function
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Questions and Answers

Which of the following is defined as the tertiary structure of a protein?

  • the primary amino acid sequence
  • structural features such as a turn
  • folded structures such as an a helix
  • structural domains such as a DNA-binding domain (correct)
  • Monomeric proteins do not contain a:

  • secondary structure
  • primary structure
  • quaternary structure (correct)
  • tertiary structure
  • Which of the following is NOT part of a zinc-finger motif?

  • proline residue (correct)
  • histidine residue
  • zinc ion
  • cysteine residue
  • There are many important roles for the dynamic nature of proteins in a cell. Which of the following is NOT likely to describe one such reason?

    <p>Quaternary structures are usually very transient (occur for short periods of time). (A)</p> Signup and view all the answers

    You are studying an oligopeptide composed of eight amino acids. The four amino acids nearest the C terminus are nonpolar. The two amino acids nearest the N terminus are charged. The middle two amino acids are polar. Which amino acid is likely to be labeled as number 2?

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

    A protein containing several proline residues is:

    <p>not likely to form alpha helices (D)</p> Signup and view all the answers

    Which of the following is true about protein folding?

    <p>Elements from the secondary structure are maintained in the tertiary structure. (C)</p> Signup and view all the answers

    When comparing domains and structural motifs, which of the following is NOT true?

    <p>Structural domains appear in different proteins with similar functions, while structural motifs have been less conserved over evolution. (C)</p> Signup and view all the answers

    You disrupt all hydrogen bonds in a protein. What level of structure will be preserved?

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

    Two proteins that have a similar function:

    <p>will share similar amino acid sequences if they are homologs (C)</p> Signup and view all the answers

    All the following statements about molecular chaperones are true EXCEPT:

    <p>they are found only in mammals (C)</p> Signup and view all the answers

    Hsp90 family members are present in all organisms EXCEPT:

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

    What role does aberrant protein folding play in the development of a disease such as Alzheimer's disease?

    <p>Misfolding and subsequent proteolytic degradation of the amyloid precursor protein generates a short fragment called b-amyloid protein, which changes from an a-helical to a b-sheet conformation. (A)</p> Signup and view all the answers

    Which of the following does NOT impose limits on protein folding?

    <p>backbone sequence of the polypeptide (B)</p> Signup and view all the answers

    Eggs are protein-rich foods. An uncooked egg can catalyze a reaction that breaks down bacterial cell walls. After cooking, this activity is almost abolished. This is likely because:

    <p>the enzyme became denatured (C)</p> Signup and view all the answers

    The correct order for molecular chaperone-mediated protein folding is:

    <p>III, II, I, IV (C)</p> Signup and view all the answers

    All the following statements about enzymes are true EXCEPT:

    <p>a single enzyme typically reacts with many different substrates (A)</p> Signup and view all the answers

    The K for an enzyme-catalyzed reaction:

    <p>is a measure of the affinity of the substrate for the enzyme (A)</p> Signup and view all the answers

    For an enzyme-catalyzed reaction, doubling the concentration of enzyme will:

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

    A small molecule that binds directly to the active site of an enzyme and disrupts its catalytic reaction is called:

    <p>a competive inhibitor (B)</p> Signup and view all the answers

    Changes in the conformational shape of an enzyme that diminish the size of its ligand-binding pocket are likely to affect an enzyme's:

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

    Which of the following is true about enzymes?

    <p>Enzymes increase reaction rates by lowering the activation energy needed to reach the transition state. (A)</p> Signup and view all the answers

    Which of the following plays a role in the degradation of proteins?

    <p>b and c (C)</p> Signup and view all the answers

    Which of the following modifications marks a protein for degradation in proteasomes?

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

    Protein self-splicing:

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

    Proteases that attack selected peptide bonds within a polypeptide chain are synthesized and secreted as inactive forms called:

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

    Which of the following is a mechanism for regulating protein activity?

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

    Protein kinase A is converted from an inactive state to an active state by binding:

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

    Kinases, which are responsible for the activation or inactivation of a number of proteins, add phosphate groups onto:

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

    The conversion of inactive chymotrypsinogen to active chymotripsin is an example of:

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

    A misfolded protein targeted to the proteasome will undergo:

    <p>unfolding using energy released by ATPases (C)</p> Signup and view all the answers

    Modification of proteins by ubiquitin and ubiquitin-like E3 ligases can stimulate all of the following EXCEPT:

    <p>mRNA stability (C)</p> Signup and view all the answers

    GTPases serve in many signal transduction pathways and the presence of GTP or GDP dictates whether the pathway is on or off, respectively. Which of the following statements is true regarding guanine nucleotide exchange factors (GEF) and their role in these signaling pathways?

    <p>They catalyze the dissociation of GDP on the G-protein to therefore promote the replacement of GTP (C)</p> Signup and view all the answers

    Which of the following methods can separate proteins based on their mass?

    <p>centrifugation and SDS polyacrylamide gel electrophoresis (C)</p> Signup and view all the answers

    In two-dimensional gel electrophoresis, proteins are first resolved by ____ and then by ____

    <p>IEF; SDS-PAGE (B)</p> Signup and view all the answers

    Gel filtration chromatography separates proteins on the basis of their:

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

    Starting with 1 mCi (milliCurie) of a phosphorus-32-labeled compound, how long would it take until only 0.125 mCi remains?

    <p>42.9 days (A)</p> Signup and view all the answers

    Western blotting is a method for detecting:

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

    A chunk of tissue is treated so that each cell's membrane is broken open to release the contents inside, and then subjected to differential centrifugation. Which of the following is true at the end of the centrifugation?

    <p>Proteins of similar density will be found in the same fraction (either pellet or supernatant) (C)</p> Signup and view all the answers

    Proteomics allows researchers to:

    <p>examine which proteins differ in abundance between a normal sample and a disease sample (C)</p> Signup and view all the answers

    Mass spectrometry techniques are used in proteomics for all of the following purposes EXCEPT:

    <p>identification of thousands of proteins' amino acid sequences within a single cell (C)</p> Signup and view all the answers

    Flashcards

    Tertiary protein structure

    The three-dimensional arrangement of a protein's polypeptide chain.

    Monomeric proteins

    Proteins composed of a single polypeptide chain.

    Zinc-finger motif

    A protein structural motif that includes a zinc ion and specific amino acid residues.

    Primary protein structure

    The linear sequence of amino acids in a protein.

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    Secondary protein structure

    Local folding patterns in a polypeptide chain, such as alpha-helices and beta-sheets.

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    Quaternary protein structure

    The arrangement of multiple polypeptide chains in a protein.

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    Coiled-coil motif

    A protein structural motif consisting of two or more alpha helices wrapped around each other.

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    Helix-loop-helix motif

    A protein structural motif consisting of two alpha helices joined by a loop.

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    Hydrophobic interactions

    Forces that drive the folding of proteins into their three-dimensional shapes.

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    Molecular chaperones

    Proteins that assist in the proper folding and assembly of other proteins.

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    Aberrant protein folding

    Incorrect protein folding that can lead to disease.

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    Enzyme

    A biological catalyst that speeds up chemical reactions in living organisms.

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    Enzyme kinetics

    The study of how enzymes function and affect reaction speeds.

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    Competitive inhibitor

    A molecule that competes with the substrate for the active site of an enzyme.

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    Proteasome

    A large protein complex that degrades proteins.

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    Ubiquitinylation

    The process of attaching ubiquitin to a protein, often marking it for degradation.

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    Zymogen

    An inactive precursor of an enzyme.

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    Proteolytic processing

    The activation of an enzyme by cleaving a portion of the inactive precursor.

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    Allosteric effector

    A molecule that binds to a protein at a site other than the active site, causing a conformational change that affects the protein's activity.

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    Positive cooperativity

    The binding of one substrate molecule increases the binding affinity of the enzyme for additional substrate molecules.

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    Two-dimensional gel electrophoresis

    A technique for separating proteins based on both their isoelectric point and molecular weight.

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    Gel filtration chromatography

    A technique that separates proteins based on their size.

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    Western blotting

    A technique used to detect specific proteins in a sample.

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    Study Notes

    Protein Structure and Function

    • Protein structure is defined by the primary, secondary, tertiary, and quaternary structures.
    • The primary structure is the amino acid sequence, linked by peptide bonds.
    • The secondary structure is stabilized by hydrogen bonds between atoms of the peptide backbone, and includes alpha helices and beta-sheets.
    • The tertiary structure is stabilized by hydrophobic interactions between nonpolar side groups and hydrogen bonds between polar side groups.
    • The quaternary structure is held together by noncovalent bonds between protein subunits.
    • Zinc-finger motifs contain a zinc ion, cysteine and histidine residues, but not proline.
    • Monomeric proteins lack the quaternary structure.

    Protein Folding

    • Proteins typically fold into specific 3D shapes determined by their amino acid sequence.
    • Hydrophobic amino acids tend to cluster in the interior, while hydrophilic amino acids are on the surface.
    • Protein folding is often aided by chaperones.
    • Hydrogen bonds, ionic interactions, and hydrophobic interactions stabilize protein folding.
    • Incorrect folding can lead to disease (e.g., Alzheimer's disease).

    Protein Function and Regulation

    • Enzymes speed up chemical reactions by lowering the activation energy.
    • The active site of an enzyme binds to a substrate and catalyzes a reaction.
    • The rate of enzyme catalyzed reaction depends on the concentration of substrate, temperature, and pH.
    • Protein folding and function are often regulated by interactions with other molecules.
    • Modification by small molecules (e.g., ubiquitination, phosphorylation) regulate protein activity.
    • Protein degradation through proteases and proteasomes is part of normal cellular processes.

    Protein Separation and Analysis

    • Methods for separating proteins include gel filtration chromatography and SDS-PAGE.
    • Two-dimensional gel electrophoresis separates proteins based on both charge and mass, allowing for a more detailed analysis of protein mixtures.
    • Mass spectrometry can identify and quantify proteins in complex mixtures.
    • Western blotting identifies specific proteins using antibodies and subsequent enzyme-based detection.

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    Related Documents

    Lodish 8e Ch03 Test Bank PDF

    Description

    Test your knowledge on the complexities of protein structure, including primary, secondary, tertiary, and quaternary formations. This quiz will also cover the process of protein folding and the role of chaperones in maintaining protein integrity. Ideal for biology students keen to understand the fundamentals of protein chemistry.

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