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26 Nov 2019

Using the Gibbs free energy equation and specific examples, explain the quantitative contributions that conformational entropy, R-group interactions and the hydrophobic effect make to the spontaneous folding of polypeptide chains into tertiary structures.

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1. Which of the following pairings regarding protein structure is/are incorrect?

Question options: a) primary structure: alpha helix

b) quaternary structure: hydrophobic interactions between different regions of the same polypeptide strand

c) tertiary structure: interactions between R groups on different polypeptide chains

d) secondary structure: hydrogen bonding between R groups on the same polypeptide strand

e) All of the above are incorrect.

2. Given the following pairs of amino acids, which pair contains the correct type of interaction through which the two amino acids most likely interact?

Question options: a) valine and leucine: charge-charge (salt bridge)

b) threonine and cysteine: disulfide bond

c) aspartic acid and glutamic acid: hydrophobic interaction

d) threonine and serine: hydrogen bonding

e) None of the above is correct.

3. Which statement is correct regarding the comparison of the following three tripeptides:

1) lys-lys-lys

2) asp-asp-asp

3) lys-asp-val

Question options:

a) Under physiological conditions, peptide #1 elutes last using cation exchange chromatography.

b) Under physiological conditions, peptide #2 elutes first using anion exchange chromatography.

c) Under physiological conditions, peptide #3 elutes last using anion exchange chromatography.

d) Under physiological conditions, peptide #3 elutes first using either cation or anion exchange chromatography.

4. When varying the substrate concentration at a fixed concentration of enzyme it is observed that at low concentrations of substrate the reaction is ________ (with respect to substrate),while at high concentrations of substrate the reaction is ________ (with respect to substrate).

Question options: a) initial; maximal

b) maximal; initial

c) second order; first order

d) first order; zero order

I need help on this chemistry work. Thanks.

DATA ANALYSIS

Using the example, calculate the Gibbs free energy for the process of dissolving ammonium nitrate and the process of dissolving sodium hydroxide (equation: ÎG = ÎH â TÎS).

Use the standard temperature 298 K.

Use the experimental data to calculate enthalpy of dissolving (ÎH).

Use the following data to calculate the entropy change (ÎS):

	S (J/K mol)
NH₄NO₃(s)	151
NH₄⁺(aq)	113.4
NO₃^-(aq)	146.4
NaOH(s)	64.46
Na⁺(aq)	59.0
OH^-(aq)	- 10.7

After completing the calculations answer the following questions separately for each experiment:

Is the dissolving exothermic or endothermic?

Does the entropy decreases or increases during dissolving?

Is the Gibbs free energy positive or negative? Is the process of dissolving spontaneous?

Using data in the appendix in your textbook, calculate Gibbs free energy for the reaction of dissolving

lithium phosphate, Li₃PO₄, in water at 25 Â°C. Do the calculations in two ways:

1) Use standard enthalpy of formation (ÎH) and entropy (S) from the appendix in your textbook, and use the same formula as you did in the lab experiments: ÎG = ÎH â TÎS. Remember that both ÎH and ÎS has to include three lithium ions.

2) Use standard free energies of formation from Appendix 6 (ÎG) and equation

ÎG = âÎG _products â âÎG _reactants

Are the results similar in both calculations?

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Using the Gibbs free energy equation and specific examples, explain the quantitative contributions that conformational entropy, R-group interactions and the hydrophobic effect make to the spontaneous folding of polypeptide chains into tertiary structures.

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