A receptor-ligand complex has a dissociation constant of Kd = 20 nM. The rate of receptor-ligand complex formation with an added ligand concentration of 10 µM is 5 × 10³ s-¹. What is the value of the reverse rate constant, k_₁?
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![added ligand concentration of 10 µM is 5 × 10³ s¹. What is the value of the reverse rate constant
k_1
=
1 ×10-4
Incorrect
Macmillan Learning
You have not correctly calculated the
value of the reverse rate constant.
To begin, calculate the value of k₁ by
dividing the rate of receptor-ligand
complex formation (the rate of the
forward reaction) by the
ligand concentration.
k₁
=
rate forward
[L]
Then, calculate the value of the reverse
rate constant, k_₁, by multiplying the
dissociation constant, Kd, and the
forward rate constant, k₁.
k_1 = Kak₁](https://content.bartleby.com/qna-images/question/049a8034-a0ab-4b8d-b3d1-3977f5f9e464/c76fa2db-7516-480c-ad08-c0ec1decc6b6/5t52jk_processed.png)
by Bartleby Expert- Crystal structures exist for three neurokinin-1 (NK1) ligand complexes with the following pdb codes (6hll, 6hlo, 6hlp) For each of the three crystal structures identify four amino acids in the NK1 binding site that contact the ligand indicating both the residue type in three letter code and the residue number. One of the chose amino acids should form a hydrogen binding interaction to the ligand, state which functional group the amino acid utilises in each caseIf intracellular [ATP] = 5 mM, [ADP] = 0.5 mM, and [Pi] = 1.0 mM, calculate the concentration of AMP at pH 7 and 25°C under the condition that the adenylate kinase reaction is at equilibrium.1E In terms of binding adenylate kinase, the Kd for ATP is ~50 M and the KI for GMP-PCP is ~50 nM. Explain how this may be possible in terms of molecular interactions. Name 4 different types of molecular interactions that may contribute to the increased binding affinity exhibited by GMP-PCP. Please help me in details
- Crystal structures exist for three neurokinin-1 (NK1) ligand complexes with the following pdb codes (6hll, 6hlo,6hlp). State which is the highest quality crystal structure indicating the criteria you used to evaluate this.a. b. C. Sphingosine-1-phosphate (SPP) has recently been discovered to be important for cell survival. The synthesis of SPP form sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence (5 µM) and absence of threo-sphingosine, a stereoisomer of sphingosine. The results are shown below. The sphingosine kinase used in all the reactions was 10 mg. Sphingosine (uM) 2.5 3.5 5 10 20 50 vo (mg. min-¹) (no inhibitor) 32.3 40 50.8 72 87.7 115.4 What are the KM and V MAX in the presence and absence of the inhibitor? What kind of an inhibitor is threo-sphingosine? What is the K₁ value? What is the Keat (turn over number)? vo (mg. min-¹) (with threo-sphingosine) 7.6 10.5 14.6 25.4 43.9 70.8affinity of a protein-protein or protein-ligand interaction can be described by the Dissociation Constant, Kd (written below). Consider a protein P and its inhibitor, I. I inhibits P's activity when bound to it: koff _ [A][B] Dissociation Constant: Ka = koN [AB] Question When [I] is 10-7 M, 99% of P's activity is inhibited. What is the Kd of this Protein- Inhibitor interaction?
- Calculate KI' of the inhibitor from the information given. All information may not be needed to calculate. K'm = (29Ki+1.45x10^-10)/Ki Vmax = 11.7 µMs-1 Kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM Inhibitor Concentration = 5x10^-12A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)Give the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.
- Calculate α' for an inhibitor with KI' = 10.0 nmol L-1 when 100 nmol L-1 of inhibitor is present.If instead of using 3.5 µM myoglobin (receptor) you used half of this (that is, 1.75 µM myoglobin), what would be that value of the Kd, that you calculated ( how would it change)? Please explain so I can solve on my own :) (How does changing concentration of the receptor in a ligand-receptor binding experiment affect the dissociation constant?)A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)