Which of these situations would produce a Hill plot with a Hill coefficient less than 1?A purified protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.A purified protein has multiple binding sites, and ligands bind to each site independently without affecting the bindingaffinity of other sites.A purified protein is a single polypeptide with one ligand-binding site, but the sample is contaminated with somepartially denatured protein molecules.A purified protein has multiple binding sites, and ligand binding to one site decreases the affinity of other sites forthe ligand.

A Hill plot is used to establish the cooperativity of ligand binding to a protein.NH (Hill…

Answered: Which of these situations would produce…

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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Similar questions

In isoelectric focusing, a protein sample is applied at the end of a gel with an immobilized pH gradient. The gel contains (high concentration, low concentration, or absence) of SDA. After application, the protein is (positively, negatively, neutrally) charged at the (high, neutral, low) pH portion of the gel.
You want to treat 10 mL of HL-60 cells with cycloheximide in order to determine the half-life of a newly discovered protein. In order to do this, the final concentration of cycloheximide needs to be 90 µM. How much of a 150 mM stock solution of cycloheximide should you add to your cells?
SDS-PAGE gels separate proteins by charge. Therefore proteins that are 10,000 daltons (g/mol) will move the same distance as proteins that are 80,000 daltons (g/mol). This statement is: True or False (And why)
Affinity chromatography You have created a fusion protein tagged with Glutathione-S-Transferase (GST). Your lab mate tells you that the affinity columns for this type of tagged protein are very similar to that of Histadine tagged proteins. Using the following elements set up a purification column and construct a protocol for an affinity purification using this tag. A large amount of glutathione is usually used to elute the tagged protein off the column. How might this work?
The binding of a ligand quenches the fluorescence of a protein. The following data were acquired: Given that the protein concentration is 0.25 μM, what is the association constant (KA) of the ligand-protein interaction? As this is a rough estimate, you do not need to report uncertainty on your result. The data pic is attached.
Some proteins migrate anomalously in SDS-PAGE gels. For instance, the molecular weight determined from an SDS-PAGE gel is sometimes very different from the molecular weight determined from the amino acid sequence. Suggest an explanation for this discrepancy.
Calculate the concentration of the ligand required to fill 25% of the binding site. X+A ⇌ XA , ka = 1.5 ×10-6 Y+A ⇌ YA , ka = 4.7 × 10-4 (i.e, q = 0.25) for both proteins.
Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the choices that apply. changes to hydrogen bonding capabilities formation of an amide bond between Cys and an isoprenyl group removal of prosthetic groups removal of the thiol group from a Cys residue modulation of charges on amino acids proteolytic cleavage covalent attachment of oligosaccharides to Asn, Thr, or Ser
Suppose that you are tasked to determine the protein concentration of an unknown protein solution via Bradford assay. You prepared six solutions of bovine serum albumin (BSA) with different concentrations. The initial concentration of the BSA stock solution is 7.50 mg/mL. Approximately 200 µL of Bradford Reagent was added to each of these solutions and the absorbance at 595 nm was taken after 5 minutes. See the table below for data on the standard solutions. Standard # A595 BSA conc (mg/mL) 0.000 0.158 2 1.125 0.291 2.250 0.372 4 3.375 0.503 5 4.500 6 5.625 0.675 Determine the protein concentration, in mg/mL, of the unknown solution if its absorbance at 595 nm was 0.248. Note: Final answer format must be x.xx (two decimal places). Round off only in the final answer. Do not round off in the middle of calculation.
Koshland, Nemethy and Filmer, proposed a model for the binding of a ligand to a dimeric protein, where the following interaction constants were introduced: KTT: KRT, KRR. Give the relationships between these constants as well as Kb1 and Kb2 during no cooperativity, positive homotropic cooperativity and negative homotropic cooperativity.
What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE? stabilizes the gel matrix, improving resolution during electrophoresis SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size. SDS raises the pH of the gel, separating multiunit proteins into individual subunits. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.
This problem concerns a "typical" tyrosine residue found on the surface of a globular protein. a) If the pKa of this residue is 10.1, at what pH will this residue be found in its deprotonated state in 99% of protein molecules? b) How would the presence of a neighboring negatively charged residue effect the equilibrium expression for the dissociation of tyrosine? c) Would the presence of the negatively charged residue raise or lower the pKa of this tyrosine? Justify and/or explain your answers in 1–2 sentences each for parts b) and c).

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