The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is \( K = 9.0 \times 10^2 \) at 310 K.**Calculate \( \Delta G \) for this reaction.****Express the Gibbs free energy to three significant figures.****Equation:**\[K_{\text{eq}} = \frac{[\text{Gly}][\text{Ala}]}{[\text{Gly-Ala}]}\]**Input Section:**- A field is provided to enter the value of \( \Delta G \) measured in kJ/mol.- Buttons for functions such as clearing input, checking answers, and accessing additional tools are included.**Submission:**- A "Submit" button is available for submitting your answer.- A "Request Answer" option is provided for further assistance.**Note:** Make sure to perform the calculation in alignment with the principles of thermodynamics, using the given equilibrium constant and temperature.

The Gibbs free energy (G) of a system is a measure of the amount of usable energy in that system.The…

Answered: The equilibrium constant for the…

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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Hydrolysis of dodecapeptide P with the enzyme trypsin affords the following fragments: Arg, Ser-Tyr-Ser-Met-Lys, Ala-Gly-Asp-Phe-Glu-Arg. Hydrolysis with chymotrypsin yields: Glu-Arg, Arg-Ser-Tyr, Ser-Met-Lys-Ala-Gly-Asp- Phe. What is the amino acid sequence of P? Submit Answer Retry Entire Group 9 more group attempts remaining
Draw the structure of alpha-ketoglutarate that is generated in a reaction catalyzed by glutamate dehydrogenase and that is a precursor to the urea cycle. You do not have to consider stereochemistry. Assume a pH of 7.
What type of polymer is being formed in Reaction #3? Name an enzyme that can catalyze Reaction #3. Is Reaction #3 favorable under mammalian cellular conditions when the concentration of dGTP is 0.2 M, dCMP is 20 mM, dGMP-dCMP is 7 mM, and PPi is 10 mM? Use △G to support your answer. Show steps
Identify and describe how you would PEGylate this peptide at its N- terminal amine. Discuss the reaction conditions you need to carry out the reaction and explain how pH affect selectivity of reaction. Draw the chemical structure of the resulting mPEG peptide conjugate.
Prepare a schematic diagram and present it as though it were a Figure in a publication (scientific journal or textbook) The diagram should illustrate the interactions made between the key components of (a) total and (b) non-specific binding reactions. In preparing your diagram，you should reflect on the role of each of the components of the reaction mixtures, and why the subtraction of non-specific from total binding allows us to calculate specific binding. The diagram Legend should be brief but informative.
Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at: a. pH 1.0 b. pH 10.1
Prepare a schematic diagram and present it as though it were a Figure in a publication (scientificjournal or textbook) (20%). The Figure should illustrate the interactions made between thekey components of (a) total and (b) non-specific binding reactions. In preparing your figure,you should reflect on the role of each of the components of the reaction mixtures, and whythe subtraction of non-specific from total binding allows us to calculate specific binding.
Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.
Draw the (B1-->A1) linked dissacharide formed between the C3 epimer of B-D-glucose and the C2 epimer of a-D-galactose. Explain in 1-2 sentences why (or why not) a precipiate would be observed when mixing this dissacharide in an alkaline solution of copper.
ΔG°′ for the isomerization reaction glucose-1-phosphate (G1P) ⇌ glucose-6-phosphate (G6P) is −7.1 kJ · mol−1. Calculate the equilibrium ratio of [G1P] to [G6P] at 25°C.
The isoelectric point (pI) of 6-phosphogluconate dehydrogenase is 6.0. Explain why the buffer used in DEAE cellulose chromatography must have a pH greater than 6 but less than 9 in order for the enzyme to bind to the DEAE resin.
The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme UTSAse (the arrow indicates the peptide bond cleaved in each case). Substrate Km(mM) kcat(s-1) PAPA↓G 4.0 26 PAPA↓A 1.5 37 PAPA↓F 0.64 18 what features of amino acid sequence dictate the specificity of the proteolytic cleavage? Large hydrophilic R-groups Large hydrophobic R-groups Neutral R-groups Small hydrophilic R-groups Large hydrophobic R-groups Negatively charged R-groups Positively charged R-groups

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The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. Keq [Gly] [Ala] [Gly-Ala]