Please help me solve 4 and explain the process. 4. Two common methods of denaturing proteins in the lab are to increase the temperature and/or addchemical denaturants like the detergent SDS (shown below). Describe how each of these processes(heating and addition of SDS) disrupts the forces and interactions that stabilize the native state, leadingto unfolding. Your answer should include a discussion of the Gibbs free energy of folding, enthalpy, andentropy.Sodium dodecyl sulfate (SDS)O-Na+MW 288

Detailed Explanation: Muscle Relaxation State:In the resting state, the muscle cell maintains a…

Answered: 4. Two common methods of denaturing…

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. The use of natural proteins as drugs requires compliance with certain storage and use conditions, which are clearly prescribed in the instructions. So, most protein preparations must be stored in a refrigerator at a temperature not excce- ding 10 °C, and dry preparations should be dissolved in boiled water cooled to room temperature. Some protein preparations are stored in hermetically scaled ampoules, from which air is removed. Why do protein drugs require strict adherence to all the conditions prescribed in the instructions, and what can happen if these conditions are violated?
Two common methods of denaturing proteins in the lab are to increase the temperature and/or add chemical denaturants like the detergent SDS (shown below). Describe how each of these processes (heating and addition of SDS) disrupts the forces and interactions that stabilize the native state, leading to unfolding. The answer should include a discussion of the Gibbs free energy of folding, enthalpy, and entropy.
2
Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, size exclusion chromatography is being done. Use the graph below and analytical methods to determine molecular weight of protein.
16. A quantitative study of the interaction of a protein with its ligand yielded the following results: Ligand concentration 0.5 1 2 3 4 5 6 9. 12 (μM) v (moles of 0.14 0.31 0.48 0.61 0.68 0.72 0.77 0.79 0.81 ligand bound per mole of protein) Plot a graph of ligand concentration versus v. Determine KD, the dissociation constant for the interaction between the protein and its ligand, from the graph.
Remember that DNA is a sequence of the letters A,C,T, and G. A binds with T and C binds with G. Solutions are specified by the DNA sequence, such as ACAC or TG, and by the concentration in units of micromolar (uM = 10-M) Consider mixing 30ml of 0.30µM ACAC with 45ml of 0.50pM TG. Predict what reactants and products should be present in the final solution and then check your answer in the virtual lab. (Please give your final answer in total nanomoles (10 moles) for each species in the solution)
1. You want to purify a protein using anion exchange column chromatography. In this technique, the solid state beads are positively charged. What charge would you want your protein to have in order for it to "stick" to the beads? Neutral Positive Negative 2. In your anion exchange experiment, your protein of interest has a pI of 6.0. Which of the following buffer solutions would you want to use when loading your protein extract onto the column so that your protein "sticks" to the beads? pH 4.5 pH 7.3 pH 6.0 3. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer consisting of 2 alpha subunits, 1 beta subunit, and 2 gamma subunits, how many bands would you expect to see on your gel? The alpha subunits are 32kDa. The beta subunit is 32kDa. The gamma subunits are 15kDa. 1 5 2 3 4. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer…
. A protein gives, under conditions of buffer composition, pH, and tem- perature that are close to physiological conditions, a molecular weight by sedimentation equilibrium measurements of 140,000 g/mol. When the same protein is studied by SDS gel electrophoresis in the absence or presence of the reducing agent B-mercaptoethanol (BME), the pat- terns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoi- chiometry of subunits, and the kinds of bonding (covalent, noncova- lent) existing between subunits. / A B - BME + BME STD Serum albumin, 67,000 Ovalbumin, 43,000 Carbonic anhydrase, 30,000 Trypsin inhibitor, 20,000 10 2. 4. Co cm migrated
1. Complete the table below with information about the amino acids utilized in this pro- cedure. Remember that smaller amino acids will travel further and so will amino acids that are soluble in the solvent. Table 9-1. Amino Acids Procedure AMINO ACIDS Phenylalanine Aspartic Acid Leucine Proline matemps DRAW THE MOLECULAR STRUCTURE in POLARITY (IS IT POLAR OR NONPOLAR?) odme her basalu la MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are false
15. The free energy of folding of a protein is -17kJ/mol. What tenoerature (C) do you have to heat the protein to unfold 10% of the proteins in solution?
H8. Protein A interacts with biomolecule B and forms a complex AB, with a dissociation constant KD = 1 µM at 25 °C, (for dissociation, AB ⇋ A + B, KD=[A][B]/[AB]). The interface contains a phenylalanine residue. A biochemist mutated the phenylalanine of protein A to a tyrosine (A’), which introduced a hydrogen bond between the hydroxyl group of the tyrosine with B without affecting any other interactions. The formation of the hydrogen bond releases a heat at 11.4 kJ/mol. What is the KD of the complex of the mutant A’ with B? Hint: Gas constant R = 8.3145 J/K/mol, Euler’s number e = 2.7183, ln(A) - ln(B) = ln(A/B).

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