C.. The formation of a hydrogen bonding dimer of N-methylacetamide has been studied as a model for hydrogenbonding in proteins. The thermodynamic parameters (at 298 K) measured for this process in water are shown below.2 H3C-NHN-methylacetamideCH3H3CHNCH3HNCH3AG° = 3.1 kcal mol-1AH° 0.0 kcal mol-1AS° -10 cal mol-1 K-1H3CN-methylacetamidehydrogen-bonded dimera) Provide a molecular level reasoning for the value of AH° and sign of ASO for this process.b) The conclusion below may be drawn from these data. Explain how his conclusion is reached.Hydrogen bonds are unlikely to be a strong stabilizing factor for a protein folding in water.c) Do you agree with this conclusion? What might be a limitation of this model for describing protein folding?d) It is well known that hydrogen bonds are prevalent in folded protein structures, so they appear to be important. So,if this conclusion is correct, what is an alternative possible role of hydrogen bonds in protein folding?

Here; is the standard change in Gibbs free energy. Any process with a negative is energetically…

Answered: C.. The formation of a hydrogen bonding…

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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Name: Date: Year/Section: Score: ACTIVITY 5.1.1 Determine the catalytic power of jack bean urease in catalyzing the hydrolysis of urea given the following conditions: At 20C, the rate constant for enzyme-catalyzed reaction is 3x104/sec The rate constant for the uncatalyzed hydrolysis of urea is 3x10-10/sec. ACTIVITY 5.1.2 Give examples of enzymatic reaction for each type of specificity 96 Copyright 2019. All Rights Reserved. 2--------
a. Describe in your own words, 5 assumptions that must be made in order to apply a Michaelis-Menten kinetic model to an enzymatic reaction. providing a mathematical expression or inequivalent (">" or "
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.
The following table shows the molecular masses (Mr) and isoelectric points (pI) of five proteins: Protein Mr pI Chicken egg white lysozyme 14,000 11.0 Carbonic anhydrase 30,000 5.4 Ovalbumin 45,000 4.5 Phosphorylase b 97,000 6.7 Lactate dehydrogenase 140,000 7.12 (a) A solution containing these five proteins was adjusted to pH 7.0 and then applied to a SIZE-EXCLUSION COLUMN. Assume that these five protein molecules are spherical in shape. Which protein is likely to be eluted LAST from the column? Explain briefly. (b) In another experiment, this protein mixture was first adjusted to pH 6.7 before applying to a CATION-EXCHANGE COLUMN. (i)What is the net charge on phosphorylase b? (ii) Which of these five proteins will bind to the CATION-EXCHANGER? Explain briefly.v
I. Buffer Preparation A researcher in Biochemistry is isolating α-glucosidase enzyme from malted wheat flour. The protocol requires the use of 2.00L of 0.225 M of lactate buffer with pH of 4.25. How will he/she prepare this buffer from 2.00 M lactic acid solution and solid sodium lactate (NaC3H5O3) The Ka of lactic acid is 1.38 x 10-4. [ Na=23.0, C=12.0, H=1.01, O=16.0 g/mol]
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. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]
Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·mol
Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…
a. What is the equilibrium constant for a reaction that is carried out at 25 °C (298 K) with H° = 20 kcal/mol and S° = 5.0 * 10 - 2 kcal mol -1 K-1? b. What is the equilibrium constant for the same reaction carried out at 125 °C?
We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
Table 2: Effect of pH on Enzyme Activity pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1 Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph. b) Over what pH range does catechol oxidase catalyze catechol to benoquinone? c) Explain why the graph has a bell-shaped curve.
The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.

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