and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29→ Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29→ Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f) What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein is able to fold normally. Intrigued by this discovery, you decide to examine this mutant more closely and discover that it has acquired a second substitution mutation at the Asp123 position. h) What amino acid(s) could be substituted for Asp123 that would allow Prot1 to retain its proper shape and function? Justify your answer

and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29→ Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29→ Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f) What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein is able to fold normally. Intrigued by this discovery, you decide to examine this mutant more closely and discover that it has acquired a second substitution mutation at the Asp123 position. h) What amino acid(s) could be substituted for Asp123 that would allow Prot1 to retain its proper shape and function? Justify your answer

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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4. Amino acids are linked together by peptide bonds to form polypeptides. (a) Draw the structure of a tripeptide (b) draw an asterisks (*) directly beside all alpha carbons and draw a square around all peptide bonds (c) Use arrows to identify and label the N-terminus and C-terminus (d) Draw a circle around the R group of each amino acid residue in the tripeptide and classify each R group as polar, non polar, acidic, or basic (e) Using the abbreviated names of the amino acids, provide the primary structure of the tripeptide you have drawn.
1.Here is an oligomeric protein, which has two binding sites:1)Write the formulas of side chains of amino acids which are located in binding sites and suggest two ligands,which can be bound with this protein. 2) Name the types of bonds which will be formed between the ligands and amino acids of binding sites.3)Give the definition of quaternary structure. What do you know about the properties of proteins with the quaternary structure?
Refer to the figure below. Replacing lysine with another amino acid in the protein may alter the shape and function of the protein. Replacing lysine with which type(s) of amino acid(s) would lead to the least amount of change in the tertiary structure of this protein? Explain.
1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?
A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain.
Our understanding of how proteins fold allows us to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might intrachain disulphide cross-linkages be formed? c)Assuming that this sequence is part of a bigger globular protein, indicate the probable location (on the surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln and Lys. Explain your reasoning
If an Arg residue in a protein was replaced with either Lys or Glu amino acid, whichsubstitution would you expect to result in the greatest structural change and why?
Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?
An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solution
1. How many different tripeptides are possible? How many carboxyl terminals of polypeptide chains are present in a molecule of hemoglobin? 2. You have isolated a pentapeptide composed of four glycine residues and one lysine residue that resides at the C-terminus of the peptide. Using the information provided in the legend of Figure 2.27, if the pK of the side chain of lysine is 10 and the pK of the terminal carboxyl group is 4, what is the structure of the peptide at pH 7? At pH 12? 3. The side chains of glutamic acid (pK 4.3) and arginine (pK 12.5) can form an ionic bond under certain conditions. Draw the relevant portions of the side chains and indicate whether or not an ionic bond could form at the following: (a) pH 4; (b) pH 7; (c) pH 12; (d) pH 13.
1. What secondary structure elements comprise each zinc finger? 2. What holds together the fold of an individual zinc finger domain?
1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.