4) For various amino acid pairs (for example: F to A, E to R, D to N, V to L, S toW), ask yourself:a) Based on what you know about the chemical properties of the side chains,what effect would you expect on the stability of the protein if you mutatedone residue of the pair into the other in the interior of the protein?What forces might have an impact on this change (ie: what types ofinteractions would you expect that amino acid to be involved in?)How would your answer change if the amino acid were located on thesurface of the protein?b)c)

Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…

Answered: 4) For various amino acid pairs (for…

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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Peptides and small proteins fold spontaneously in aqueous solution at room temperature. Thus, for a small protein in water, we can say ΔG FOLD < 0. Denoting the unfolded protein as Unf and the folded protein as Fld, we can write the following equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering the transition from the unfolded state (in which there are many possible conformations) to the folded state (only one conformation), there is clearly a decrease in the entropy of the protein. However, protein folding is (correctly) described as an entropically driven process.a) Resolve this apparent paradox by identifying the enthalpy (ΔH) and entropy (−TΔS)components involved in protein…
3b) Both a-helical 2° structure and b-pleated sheet 2° structure result from the same type of interaction; briefly explain in your own words why you might observe an a-helix in one region of a protein and a b-pleated sheet in another region of the same protein.
Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.
5 (a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
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.
Describe the forces that are involved in the tertiary structure of a protein and give an example of each force listed.
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.
Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.
Provide the number of polypeptide chains present andthe number of amino acid residues in each chain. for https://www.rcsb.org/structure/6j20 Provide the molecular weight of the protein orprotein complex and the total number of atoms. (All of this information can be found in the PDBpage.) Create a figure (available in the PDB page) that shows the topology of your protein, i.e.the secondary structures adopted by different regions of the protein (alpha helix, beta strand).Make sure to also provide a figure legend that helps interpret the figure and appropriate figurecaption that briefly explains the figure.
how does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on the surface of a protein 3. an asparate chain in a hydrophobic pocket adjacent to a glutamte side chain 4. an asparate side chain in a hydrophobic porket adjacent to a lysine side chain.
a) From the chemical structure above, write the amino acid sequence using both three-letter and one-letter abbreviations. Disregard chirality for this question. b) Indicate adjacent to the alpha-carbon of each residue whether it has an L- or D-configuration.
19.40 Indicate whether each of the following statements describes the primary, secondary, tertiary, or quaternary protein structure: a. Hydrophobic amino acid residues seeking a nonpolar envi- ronment move toward the inside of the folded protein. b. Hydrophilic amino acid residues move to the polar aqueous environment outside the protein. c. An active protein contains four tertiary subunits. d. In sickle cell anemia, valine replaces glutamate in the B-chain.

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