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for each of the proteins beliw
the circles denote a folded Polypeptide and the red lines...
3. Suppose the polypeptide below (where each circle represents an amino acid residue) was to form...
3. Suppose the polypeptide below (where each circle represents an amino acid residue) was to form a folded structure stabilized primarily by a disulfide linkage. a. Draw the folded structure (using circles) and illustrate the disulfide bond. Asp Met LeuCys Gly GlyY Val IleTyrXSerVal CysPhe b. What level of protein structure is being illustrated in the folded forrm? Primary, secondary, tertiary, or quaternary? c. What other type of intramolecular interaction might stabilize the folded form of this polypeptide? 4. The...
Question 6 Which of the following statements regarding a protein with 4 domains must be true?...
Question 6 Which of the following statements regarding a protein with 4 domains must be true? A protein with 4 domains must have 4 different kinds of secondary structures. O A protein with 4 domains must be composed of 4 polypeptide chains. A protein with 4 domains must have 4 regions that fold independently. A protein with 4 domains must have a quaternary structure. Question 7 Histone proteins are typically... o rich in disulfide bonds O composed of a random...
26. Which of the following classification does not match the amino acid side chain A) Contains an basic group/ lysi...
26. Which of the following classification does not match the amino acid side chain A) Contains an basic group/ lysine B) It is polar C) Forms disulfide bond/ cysteine D) Forms hydrogen bonds with neighbors/ alanine serine 27. All amino acids found in proteins are L-amino acids EXCEPT the achiral. A) glutamate B) Lysine C) glyeine D) Alamine 28. The plH at which the positive and negative charges of an amino acid balance each ofher is called the A) isotonic...
5. (12 Points) We learned that larger proteins may have specific domains that contribute to catalytic...
5. (12 Points) We learned that larger proteins may have specific domains that contribute to catalytic activity of an enzyme. In most cases, the independent isolated domains can be separated and will remain folded in solution. In the context of a full length protein, these domains are interconnected within the protein by flexible loops. An example enzyme protein (EX-FL) has a peptide bond cleaved between two residues to produce two fragments, a peptide fragment (20 residues in length, EX-pep) and...
Hemoglobin consists of four globular proteins, each formed from a polypeptide chain. Each globular protein contains...
Hemoglobin consists of four globular proteins, each formed from a polypeptide chain. Each globular protein contains a nonprotein group with an iron ion. This iron ion binds to an oxygen molecule. Thus, every hemoglobin protein can bind four oxygen molecules. Select the correct statement about oxygen transport below. a. Myoglobin transports oxygen through the bloodstream to tissue. b. To carry oxygen, iron must be in its nonheme form. c. Erythrocytes contain abundant myoglobin for transporting oxygen. d. Hemoglobin is found...
SULR as the fow thermometer un 2. When a protein denatures in a cell, what causes...
SULR as the fow thermometer un 2. When a protein denatures in a cell, what causes it to aggregate with other denatured cell proteins? (2pts) 3. How might a heat shock protein help a protein fold correctly in a cell under normal conditions? (2 pts). 4. The bacterial GroEL heat-shock protein and the plant Rubisco assembly proteins are said to be homologous proteins. What is it about these proteins that has caused them to be described as members of the...
2 points Which of the statements below is false? * O The genetic code is universal....
2 points Which of the statements below is false? * O The genetic code is universal. Degenerate codons specify the same amino acids. The genetic code is overlapping. O The genetic code is triplet. 2 points How many hydrogen bonds does cytosine form with guanine? * 2 3 O 4 2 points The amino acid sequence of a polypeptide chain comprises the structure of the protein. * primary secondary tertiary O quaternary 2 points One gene can have multiple effects...
Question 5. Which of the following pairs of bonds within a peptide backbone show free rotation...
Question 5. Which of the following pairs of bonds within a peptide backbone show free rotation around both bonds? A) Ca-C and N-C B) C-O and N-C C) C-O and N-Ca D) N-C and Ca-C E) N-Ca and N-C Question 6. In the diagram below, the plane drawn behind the peptide bond indicates the: A) absence of rotation around the C-N bond because of its partial double-bond character. B) plane of rotation around the C-N bond. region of steric hindrance...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular weight of the native (undenatured) protein was 130,000 dalton. His advisor wanted him to determine whether this protein had quaternary structure using gel electrophoresis. He wants to be able to describe the molecular weight of each of the subunits and the forces involved in linking these subunits together (disulfide linkages and/or electrostatic, hydrogen bonding and hydrophobic interactions). Carl first analyzed his pure protein sample...
las n o relationship with the tertiary structure. nuclease proves that the primary structure of a...
las n o relationship with the tertiary structure. nuclease proves that the primary structure of a globular the he d) The planes of base pairs using ribo e) Th rs are parallel to the helix axis in the Watson-Crick DNA double helix. e sequence on one strand of n Crick DNA doubld e the helix varies independenty of that in the other strand in the varies in 10. The person n that discovered that A:T and G:C ratios in DNA...
3. Suppose the polypeptide below (where each circle represents an amino acid residue) was to form a folded structure stabilized primarily by a disulfide linkage. a. Draw the folded structure (using circles) and illustrate the disulfide bond. Asp Met LeuCys Gly GlyY Val IleTyrXSerVal CysPhe b. What level of protein structure is being illustrated in the folded forrm? Primary, secondary, tertiary, or quaternary? c. What other type of intramolecular interaction might stabilize the folded form of this polypeptide? 4. The...
Question 6 Which of the following statements regarding a protein with 4 domains must be true? A protein with 4 domains must have 4 different kinds of secondary structures. O A protein with 4 domains must be composed of 4 polypeptide chains. A protein with 4 domains must have 4 regions that fold independently. A protein with 4 domains must have a quaternary structure. Question 7 Histone proteins are typically... o rich in disulfide bonds O composed of a random...
26. Which of the following classification does not match the amino acid side chain A) Contains an basic group/ lysine B) It is polar C) Forms disulfide bond/ cysteine D) Forms hydrogen bonds with neighbors/ alanine serine 27. All amino acids found in proteins are L-amino acids EXCEPT the achiral. A) glutamate B) Lysine C) glyeine D) Alamine 28. The plH at which the positive and negative charges of an amino acid balance each ofher is called the A) isotonic...
5. (12 Points) We learned that larger proteins may have specific domains that contribute to catalytic activity of an enzyme. In most cases, the independent isolated domains can be separated and will remain folded in solution. In the context of a full length protein, these domains are interconnected within the protein by flexible loops. An example enzyme protein (EX-FL) has a peptide bond cleaved between two residues to produce two fragments, a peptide fragment (20 residues in length, EX-pep) and...
SULR as the fow thermometer un 2. When a protein denatures in a cell, what causes it to aggregate with other denatured cell proteins? (2pts) 3. How might a heat shock protein help a protein fold correctly in a cell under normal conditions? (2 pts). 4. The bacterial GroEL heat-shock protein and the plant Rubisco assembly proteins are said to be homologous proteins. What is it about these proteins that has caused them to be described as members of the...
2 points Which of the statements below is false? * O The genetic code is universal. Degenerate codons specify the same amino acids. The genetic code is overlapping. O The genetic code is triplet. 2 points How many hydrogen bonds does cytosine form with guanine? * 2 3 O 4 2 points The amino acid sequence of a polypeptide chain comprises the structure of the protein. * primary secondary tertiary O quaternary 2 points One gene can have multiple effects...
Question 5. Which of the following pairs of bonds within a peptide backbone show free rotation around both bonds? A) Ca-C and N-C B) C-O and N-C C) C-O and N-Ca D) N-C and Ca-C E) N-Ca and N-C Question 6. In the diagram below, the plane drawn behind the peptide bond indicates the: A) absence of rotation around the C-N bond because of its partial double-bond character. B) plane of rotation around the C-N bond. region of steric hindrance...
las n o relationship with the tertiary structure. nuclease proves that the primary structure of a globular the he d) The planes of base pairs using ribo e) Th rs are parallel to the helix axis in the Watson-Crick DNA double helix. e sequence on one strand of n Crick DNA doubld e the helix varies independenty of that in the other strand in the varies in 10. The person n that discovered that A:T and G:C ratios in DNA...
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