How can the dissociation equilibrium constant, and the total number of receptors be calculated from a binding curve in a radiolabeled ligand saturation assay?

An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are:     a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare

Based on your Lineweaver-Burk plot, what is the mode of PaESBL-1 inhibition by NSAMB? What is the equation for the double-reciprocal plot at 20 nMnM NAMB?

Transition-state analogs, which can be used as enzyme inhibitors and to generate catalytic antibodies, are often difficult to synthesize. Suggest a reason.

From this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions.   Parameters required for calculation of coefficient (Kd) for unknown protein   Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo

a) What is the KDD​ for this myoglobin variant? b) What is the predicted fractional saturation for the last box in the table? (please show your work so I can better understand) c) What is unexpected about the binding curve above? (5 words or less) d) What must be structurally different about this new variant relative to other known Myoglobin variants to generate this graph?

A variety of organic chelating ligands have been synthesized to tightly coordinate radioactive metal cations to identify and treat malig- nancies by coupling the metal complex to a polypeptide linker attached to a monoclonal antibody that binds specifically to a cell surface re- ceptor. One such metal complex is illustrated in the diagram on the right. The radioactive Cu-64 cation is tightly coordinated by the che- lating ligand that is, in turn, conjugated to a peptide linker attached to a monoclonal antibody. (The antibody is not shown in this diagram.) When coupled to a specifically designed monoclonal antibody, the complex binds specifically to somatostatin receptors that are ex- pressed on the surface of neuroendocrine tumors. Subsequently the entire complex with the receptor is internalized, i.e., passed into the cytoplasm, where the radioactive metal cation kills the malignant cell. 1. CH3 HN NHNH HN NHNH HN Но НО NH HN S-S HN Но NH NH HN -NH HN- H2N OH NH ) Write the three…

The dissociation equilibrium constant (Kd) is:_____ (select all that apply) Group of answer choices: Is a measure of ligand efficacy Typically equivalent to 1- Ka The concentration of ligand that gives maximal receptor occupancy The concentration of ligand that gives half-maximal receptor occupancy Measured in 1/M or M-1 Typically measured in mol/L or M A measure of the strength of a ligand - receptor binding reaction

You were recently tasked with the responsibility of generating an aptamer that was capable of binding to protein K with high specificity. a) Describe how you would utilize methods such as SELEX to identify aptamer candidates with the desired property. b) Assuming that aptamer binding was dependent on the presence of a bound Mg2+ (no metal binding site on protein K) describe how you would account for this metal binding requirement in your SELEX workflow.

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.