3. Consider Anfinsen's classical protein folding experiment.SHG=ANative(100% active)ĞNative1. Reduce2.8 M urea1. Reduce2.8 M ureaSHSHHSDenatured(inactive)SHSHSHSHSHDenatured1. Remove urea2. Oxidize1. Oxidize2. Remove ureaABa. What do you expect to be the results of Experiment A versus Experiment B above. Explain.b. In Anfinsen's experiment, the Ribonuclease protein will fold correctly even if kept in a reducingenvironment (all disulfide bonds broken). What are the main driving forces that lead to properfolding?c. What is the main force that opposes folding?

The experiment that Anfinsen conducted to establish the classical folding of proteins proved that…

Answered: 3. Consider Anfinsen's classical…

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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I am not understanding why TA of alcohol precipitation is used as TA of purified protein. I provided 2 photos, 1 with the questions and the correct answer, and the other photo is a screenshot of the explanation.
10. A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the physiological protein has a molecular weight of 240,000 Daltons. Chromatography in the presence of 6 M urea yields a single peak corresponding to a protein of 60,000 Daltons. Chromatography in the presence of 6 M urea and 10 mM mercaptoethanol yields peaks for proteins of 34,000 Daltons and 26,000 Daltons. What can we learn about protein's tertiary and quaternary structure from this data?
9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2
Why does in this experiment, after gel is formed from gelatin the marble in papaya juice to the first cup (Lot A), second cup (Lot B) and 10 ml of kiwi juice to the third cup (Lot C) disappeared? While in fourth cup (control) the marble did not disappear it just float on the surface. What is the action of protease on gelatin?
4. Deducing quaternary structure via SDS-PAGE. SDS-PAGE is a convenient method for separating polypeptides solely on the basis of size. Small polypeptides travel faster than large ones; rate of migration through the gel is inversely proportional to the logarithm of molecular weight. The subunit structure of a multimeric protein often can be deduced using this technique in conjunction with a protein cross-linking agent. Cross-linking agents react with amino acid residues of two polypeptides that are in contact, thereby linking them by covalent bonds. After limited treatment with the reagent, so that some but not all subunits become cross-linked to their neighbors, the protein is subjected to SDS-PAGE and the molecular weights of the resulting proteins (bands) are estimated. The results of such experiments on two proteins (Protein A and Protein B) are shown below. What is the most likely subunit structure of each protein? Protein A SDS-PAGE cross-linking agent MW 105,000 70,000 35,000…
Indicate which of the following descriptions is true about the biochemical depicted here: NH₂ +41 5 HO- он он OH OH OH a. Ribonucleotide b. Complementary to dTTP c. Purine d. Key reagent in Sanger sequencing e. Answers b., c. and d. are correct
Help please
1. In the mechanism of action of triose phosphate isomerase, Lys12 is an essential amino acid in the flexible phosphate gripper loop that undergoes a large conformational change to trap the substrate in the active site excluding water and holding the phosphate group in the correct geometry for isomerization rather than dephosphorylation. What would be the effect of the mutation of Lys12 to the unusual amino acid shown below? Explain. protein backbone
13. Amino acid analysis of a seven residue long peptide gave Asp Leu Arg Met | Phe Met | Phe | Tyr (i) The PTH amino acid derivative released by Edman degradation was Tyr-PTH (ii) Trypsin treatment had no effect (iii) Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Arg (iv) Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Arg, and Met What is the amino acid sequence of this seven residue long peptide, and explain how you reached that conclusion?

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