=20 nM. The rate of receptor-ligand complex formation with anA receptor-ligand complex has a dissociation constant of Kaadded ligand concentration of 10 µM is 5 × 10³ s¯¹. What is the value of the reverse rate constant, k_₁ ?k_₁=8-1

The dissociation constant (Kd) for a receptor-ligand complex is related to the rate constants for…

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?

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?

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

See similar textbooks

Related questions

Q: Consider a uniport system where a carrier protein transports an uncharged substance A across a cell…

A: ∆G = R T ln (Ainside /Aoutside) Where G is free energy change for the transport of uncharged…

Q: Which of the following must be true based on the data below for ligand L binding to protein A and to…

A: Proteins are biomolecules which catalyzes most of the biochemical reactions in all living cells and…

Q: (d) ( through the disulfide bridge. If this bridge were found for the two joined amino acids free in…

A: Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Q: the reduced electron carrier that enters Complex II of the electron transport chain, downstream of…

A: Energy is needed by the cell to do work. The energy is produced by oxidizing the glucose molecules…

Q: The figure shows binding curves for two proteins that bind the same ligand. Which binding curve…

A: Ligand binding curve: this is also called as saturation curve that shows the fraction Y of protein…

Q: The Structure of the acetylcholine receptor is shown below: A. Knowing the amino acid sequence of…

A: All amino acids are of different property based on their property they present on the cytoplasmic…

Q: Molecular diameters of proteins IgG and TNFα are 11.2 nm and 4.4 nm, respectively. The diffusion…

A: Stokes-Einstein equation is the relationship between radius and diffusion coefficient of a substance…

Q: Given the melting profile of a membrane bilayer consisting of (see attached diagrams) where R =…

A: The graph here has degree of fluidity as Y-axis and temperature as X-axis. The curve will shift to…

Q: 1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value…

A: Cooperativity or cooperative binding occurs when binding of one molecule influences the affinity of…

Q: the number of low affinity binding sites occupied by a ligand at 100% saturation is greater than the…

A: Introduction A molecule that particularly attaches to another molecule, often a bigger one, is known…

Q: To better understand how the lacR works, let's start let's approximate the volume of a bacterial…

A: The bacterial cell is considered as a cylInder. The equation to find volume of cylinder is ''.

Q: The fatty acid side chains of the phospholipids in the inner mitochondrial membrane exhibit a large…

A: Since you have posted multiple questions, we will provide the solution only to the first question as…

Q: Which ligand-binding curve in the figure below would be consistent with the protein exhibiting a Ka…

A: Consider the interaction between a protein (P) and ligand (L) as shown below.Here, Ka is the…

Q: Crystal structures exist for three neurokinin-1 (NK1) ligand complexes with the following pdb codes…

A: NK1 is a type of mammalian tachykinin receptors. These are G-protein coupled receptors which are…

Q: The

A: Introduction: The nervous system, a complex network of specialized neurons and supporting cells…

Q: Can you explain the experimental procedure from this article? Please explain as if your having…

A: In this work, the role of inositol 1,4,5-trisphosphate receptor (InsP3R) and Na, K-ATPase in the…

Q: Members of the integrin family are the major cell surface receptors for many ECM proteins such as…

A: Integrins are a family of αβ heterodimers. Integrins are cellular adhesion receptor molecules that…

Q: A new protein namely protein X has been isolated by molecular biologists. The protein is shown to…

A: Protein: Proteins are necessary nutrients for human health. They are a component of body tissue and…

Q: The alpha subunit of the heterotrimeric G-protein complex becomes activated upon activation of a…

A: Introduction: G Protein-coupled receptor (GPCR) also known as serpentine receptors or seven-pass…

Q: Give an example of a protein containing primarily betapleated sheets. Is this a fibrous or globular…

A: Protein structure decides the amino acid sequence, chemical bonds found between atoms in the…

Q: Hormone A binds to its receptor with a KL of 5 μM. In the presence of 2.5 μM compound B and 2.0 μM…

A: A ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. In…

Q: Substrate A has a Km of 45uM and a kcat of 100/s with trypsin and a Km of 540mM and a kcat of 2/s…

A: Enzymes are the proteinous structure that helps in increasing the rate of metabolism. The function…

Q: In a Myoglobin and azide ligand-receptor binding experiment, instead of using 3.5 µM myoglobin you…

A: Myoglobin acts as oxygen reserve in the muscle cells. Myoglobin (Mb) has higher affinity towards…

Q: Given that the protein concentration is 0.25 μM, what is the association constant (KA) of the…

A: Fluorescence is a luminescence technique used in fluorescent labeling and fluorescence spectroscopy…

Q: Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and…

A: ANSWER;- It is given that the ka values of OBP and elephants Hb are the same at pH=7. Kd is the…

Q: A galvanic cell at a temperature of 25.0 °C is powered by the following redox reaction: 2+ 2+ Sn(aq)…

A: To calculate cell voltage of galvanic cell under given conditions , we need to use Nernst…

Q: An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds…

A: The equilibrium constant, K, expresses the relationship between a reaction's products and reactants…

Q: Provide a brief explanation as to why ligand binding to proteins must be a reversible process.

A: A protein–ligand complex is a complex made up of a protein and a ligand that forms as a result of…

Question

=
20 nM. The rate of receptor-ligand complex formation with an
A receptor-ligand complex has a dissociation constant of Ka
added ligand concentration of 10 µM is 5 × 10³ s¯¹. What is the value of the reverse rate constant, k_₁ ?
k_₁
=
8-1

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1: Dissociation constant (Kd)

VIEW

Step 2: Conversion of unit from nM to M

VIEW

Solution

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 3 steps

SEE SOLUTION Check out a sample Q&A here

Follow-up Questions

Read through expert solutions to related follow-up questions below.

Follow-up Question

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

Solution

by Bartleby Expert

SEE SOLUTION

Similar questions

What effect does a negative effector have on the graph of reac- tion rate (V) vs. [substrate] for an allosteric effector?
In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to the Hill coefficient
A sample of a protein is analyzed by CE using a neutral-coated capillary with a total length of 25.0 cm and a distance to the detector of 22.0 cm. Using an applied voltage of 20.0 kV, the protein was detected at a migration time of 16.2 min. The diffusion coefficient for the protein is 2.4 x 10-7 cm?/s. (a) Calculate the apparent electrophoretic mobility of the protein. (b) Calculate the expected number of theoretical plates for the analysis.
A 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)
Two proteins, A and B, bind to the same ligand, L, with the binding curvesshown below. What is the dissociation constant, Kd , for each protein? Which protein (A or B) has a greater affinity for ligand L?
List 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms
The CMC of SDS is 8.2 mM at 25 °C. Please describe the biological membrane solubilization when [SDS] is below or above 8.2 mM in the solution.
The order is for Ceftin 0.25 gPO, bid. On hand you have Ceftin 125mg tablets. How many tablets should you give?
Calculate θ for a certain protein-ligand pair when the ligand concentration = 1 M and the Kd = 1 X 10-15 M.
Suppose the major solutes in intact lysosomes are KCl (~0.1 M) and NaCl (~0.03 M). When isolating lysosomes, what concentration of sucrose is required in the extracting solution at room temperature (25oC) to prevent swelling and lysis? Calculate how much sucrose (342.3 g/mol) would you need to make 500 ml of this extracting solution.