14.2 50. A transport protein is known to have the following structure: a prosthetic group carries reduced iron while one moiety iscomposed of two alpha subunits and two beta subunits. These components come together in order to form the largerfunctional protein. Based on this information, what is the level of protein structure being described?A. Primary structure; the moieties simply refer to the amino acid chain that has a particular sequence.B. Secondary structure; the moieties are highly irregular in their arrangement.C. Tertiary structure; the polypeptide chains are arranged in geometrically ordered units.D. Quaternary structure; the protein is formed by tetramers that are interlocked with one another.51. What will initially change in an amino acid chain being synthesized in a cell if there was a point mutation?|- amino acid sequenceIl - amino acid compositionIII - hairpin loopIV - pseudoknotA. Choice I onlyB. Choices I and IIC. Choices I, II, and III

A peptide bond that holds a linear chain of amino acids together is known as Protein. Protein has…

Answered: 50. A transport protein is known to…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..
29. What distribution of amino acids would you expect to find in a protein embedded in a lipid bilayer.
81. You have used the primary amino acid sequence of a newly identified protein (of unknown function) to make a hydropathy plot. From this plot you believe it might be a transmembrane receptor. This is because the plot tells a. the secondary structure is likely made up of several B sheets. b. the secondary structure is likely made up of a-helices. c. the protein would be readily hydrolyzed if in an aqueous environment. d. on average, there are a lot of hydrophobic amino acids in the protein. e. there are several hydrophobic areas interspersed with short hydrophilic stretches. you that 82. You are studying a mutant type of garter snake known for its odd slithering movement. You isolated the mutated gene and this morning you just got the results from your DNA sequencing. What would be your first step towards determining the potential function of the protein encoded by this gene? a. Use X-ray crystallography to determine the tertiary structure of the protein. b. Use computer programs that…
Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acids
11. Below is a folding energy funnel describing folding energy landscape of a protein. The width of the funnel indicates the entropy of the protein, and the height corresponds to the free energy. A) If A is the native fold structure, which state is a molten globule? How does this state differ from A in term of structures. B) Does this protein have multiple folding pathways or just one? C) which state has the lowest free energy? D) According to the width of the funnel, the native state B of the protein has the lowest entropy. If the protein fold A spontaneously to this state, does it violate the 2nd law of thermodynamics? Why or why not? (Hint: in the folding funnel, only the entropy of the protein alone is considered). E) Does the native state also have the lowest enthalpy. What makes the enthalpy decrease as the protein folds? 12. List four methods by which a protein can be denatured and briefly describe how these methods act to disrupt protein structure.
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R
Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?
9. A) Please write down the names of the following protein folds. A B C B) Which one(s) is made of more than one polypeptide? D E 000 C) Give an example of a protein containing the motif in C and explain how the structure of this motif facilitates function. 10. What is Levinthal's paradox? Describe the paradox and explain the conclusion to which it led.
Explain how both alpha helices and beta sheets can be used by proteins that cross membranes. Also explain what a hydropathy plot is and how such a plot can be used to differentiate transmembrane alpha helices from transmembrane beta sheets.
In the article the authors reference the canonical forces in protein folding. Describe how these forces make folding an energetically favorable process. Why do the authors suggest that other intermolecular interactions must be important to fully understand folding processes?
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…

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