Homework Answers
6) D
A protein with 4 domain must have a quartenery structure.
Eg :- Haemoglobin
Consist of 2 alpha and 2 beta subunits and globin fold with heme pocket.
7) D
Histone proteins are rich with positively charge amino acid lysine , arginine and histidine.
8)B
Unique sequences is a stretch of DNA present only a single copy in a cell.
9)B
Each nucleosome contain 2 copies of each histone protein ( H2A,H2B,H3,H4).
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Question 6 Which of the following statements regarding a protein with 4 domains must be true?...
Which of the following statements are true about protein domains? I. Polypeptide chains longer than 200...
Which of the following statements are true about protein domains? I. Polypeptide chains longer than 200 amino acids in length have multiple domains. II. Domains are tertiary structural components of proteins. III. Different domains are encoded by different exons of a gene. IV. Each domain in a protein has a specific function. A. I, II, III, and IV B. I, II, and III C. II, III, and IV D. II and IV E. I and IV
b and d please. c is an example 3. (25 points) You have predicted the amino...
b and d please. c is an example
3. (25 points) You have predicted the amino acid sequences of several proteins based on their open reading frames. The significant domains are shown below. Diagram the final localization(s) (only as far as the ER or nucleus) and any orientation of domains for each protein. Also, indicate all regions that could be GLYCOSYLATED for each protein. No explanation needed if diagrammed and labeled clearly. Empty rectangle = 25 amino acid hydrophobic-rich sequence...
1. Which of the following statements is consistent with the structural motifs in 1OPF? This protein...
1. Which of the following statements is consistent with the
structural motifs in 1OPF?
This protein has tertiary structure, where each subunit is a
large parallel beta barrel.
This protein has quaternary structure, where each subunit is a
large antiparallel beta barrel.
This protein has tertiary structure, where each subunit is a
large antiparallel beta barrel.
This protein has quaternary structure, where each subunit is a
large parallel beta barrel.
3. Given the information in the PDB entry for 1OPF,...
please answer all. 14. [6 pts) Indicate which of the following statements is True (T) or...
please answer all.
14. [6 pts) Indicate which of the following statements is True (T) or False (F) When water interacts with hydrophobic molecules, it becomes more ordered and entropy of the system increases The hydrophobic effect is predominant in protein stability The Ramachandran ploy shows combinations of dihedral angles in a polypeptide chain. A proteins function is directly related to the protein's secondary structure. The B sheet is primarily stabilized by R group interactions Clusters of secondary structures are...
Indicate whether the following statements are true or false. Items (6 items) (Drag and drop into...
Indicate whether the following statements are true or false. Items (6 items) (Drag and drop into the appropriate area below) Protein folding releases energy to the surroundings (AG<0). All proteins are made of amino acids. All proteins require chaperones to fold. All proteins have disulfide bonds. Unfolded RNaseA cannot be refolded. "Molten globule" describes the initial stages of protein folding in which the conformation is still very dynamic. Categories True True False
QUESTION 3 Domains are A independently folded regions of a protein that are evolutionarily conserved O...
QUESTION 3 Domains are A independently folded regions of a protein that are evolutionarily conserved O Bare found only in proteins with a high percentage of beta sheet content • Care highly sensitive to amino acid residue mutation • D. are only alpha-helical QUESTION 4 Protein folding is guided by energy and entropy considerations. The native structure of a protein exhibits low energy. low entropy low energy, high entropy high energy, high entropy high energy low entropy
6. If you have two proteins with unknown concentrations (4 points): -sample A: a protein that...
6. If you have two proteins with unknown concentrations (4 points): -sample A: a protein that contains polar uncharged amino acids, negatively charged amino acids and arginines, size: 40 KDa -sample B: a protein rich in lysines, size: 100 KDa A. If you want to separate both proteins, which acrylamide gel concentration would you chose? B. Which staining method (s) would you chose for this gel? Why?
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...
6. (4) You are trying to make a synthetic copy of a particular protein but accidentally...
6. (4) You are trying to make a synthetic copy of a particular protein but accidentally join the amino acids together in exactly the reverse order. One of your classmates says the two proteins must be identical, and bets you $20 that your synthetic protein will have exactly the same biological activity as the original. After having read this chapter, you have no hesitation in staking your $20 that it won’t. What particular feature of a polypeptide chain makes you...
You are growing cells in the lab and want them to express Protein X. You have...
You are growing cells in the lab and want them to express Protein X. You have added all necessary transcription factors (both general and specific and have checked all regulatory sequences for mutations (there are none). Still, transcription is not occurring. The best explanation for this would be... The cell is missing a HAT (histone acetyltransferase) O The cell is missing a DNA polymerase O The cell is missing an HMT (histone methyltransferase) The cell is missing an HDAC (histone...
b and d please. c is an example
3. (25 points) You have predicted the amino acid sequences of several proteins based on their open reading frames. The significant domains are shown below. Diagram the final localization(s) (only as far as the ER or nucleus) and any orientation of domains for each protein. Also, indicate all regions that could be GLYCOSYLATED for each protein. No explanation needed if diagrammed and labeled clearly. Empty rectangle = 25 amino acid hydrophobic-rich sequence...
1. Which of the following statements is consistent with the
structural motifs in 1OPF?
This protein has tertiary structure, where each subunit is a
large parallel beta barrel.
This protein has quaternary structure, where each subunit is a
large antiparallel beta barrel.
This protein has tertiary structure, where each subunit is a
large antiparallel beta barrel.
This protein has quaternary structure, where each subunit is a
large parallel beta barrel.
3. Given the information in the PDB entry for 1OPF,...
please answer all.
14. [6 pts) Indicate which of the following statements is True (T) or False (F) When water interacts with hydrophobic molecules, it becomes more ordered and entropy of the system increases The hydrophobic effect is predominant in protein stability The Ramachandran ploy shows combinations of dihedral angles in a polypeptide chain. A proteins function is directly related to the protein's secondary structure. The B sheet is primarily stabilized by R group interactions Clusters of secondary structures are...
Indicate whether the following statements are true or false. Items (6 items) (Drag and drop into the appropriate area below) Protein folding releases energy to the surroundings (AG<0). All proteins are made of amino acids. All proteins require chaperones to fold. All proteins have disulfide bonds. Unfolded RNaseA cannot be refolded. "Molten globule" describes the initial stages of protein folding in which the conformation is still very dynamic. Categories True True False
QUESTION 3 Domains are A independently folded regions of a protein that are evolutionarily conserved O Bare found only in proteins with a high percentage of beta sheet content • Care highly sensitive to amino acid residue mutation • D. are only alpha-helical QUESTION 4 Protein folding is guided by energy and entropy considerations. The native structure of a protein exhibits low energy. low entropy low energy, high entropy high energy, high entropy high energy low entropy
6. If you have two proteins with unknown concentrations (4 points): -sample A: a protein that contains polar uncharged amino acids, negatively charged amino acids and arginines, size: 40 KDa -sample B: a protein rich in lysines, size: 100 KDa A. If you want to separate both proteins, which acrylamide gel concentration would you chose? B. Which staining method (s) would you chose for this gel? Why?
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...
You are growing cells in the lab and want them to express Protein X. You have added all necessary transcription factors (both general and specific and have checked all regulatory sequences for mutations (there are none). Still, transcription is not occurring. The best explanation for this would be... The cell is missing a HAT (histone acetyltransferase) O The cell is missing a DNA polymerase O The cell is missing an HMT (histone methyltransferase) The cell is missing an HDAC (histone...
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