Answer all questions. The E1 component contains active sites/s at the interface of thesubunits.1: alpha and beta2; alpha and beta2; alpha and alpha1; alpha and alphaWhich of the following interactions contribute to the binding of TPW (the thiamine pyrophosphate analog)?Ohydrogen bondsOpi stackingO coordinate bonds, or metal interactionsAll of these interactions contribute to the binding of TPW.The E1 component of the PDC is best described as anOa₂B2Y1₁ heterotetramera₂ß2 homotetramerOa2ß2 heterotetramera2ß2Y1 heteropentamer

E1 catalyzes pyruvate decarboxylase. It contains 1 alpha active sides at the interface of beta…

The E1 component contains active sites/s at the interface of the subunits. 1: alpha and beta O2; alpha and beta 2; alpha and alpha O1: alpha and alpha Which of the following interactions contribute to the binding of TPW (the thiamine pyrophosphate analog)? Ohydrogen bonds pistacking O coordinate bonds, or metal interactions All of these interactions contribute to the binding of TPW. The E1 component of the PDC is best described as an Oa₂B2Y1 heterotetramer Ⓒa₂ß₂ homotetramer

The E1 component contains active sites/s at the interface of the subunits. 1: alpha and beta O2; alpha and beta 2; alpha and alpha O1: alpha and alpha Which of the following interactions contribute to the binding of TPW (the thiamine pyrophosphate analog)? Ohydrogen bonds pistacking O coordinate bonds, or metal interactions All of these interactions contribute to the binding of TPW. The E1 component of the PDC is best described as an Oa₂B2Y1 heterotetramer Ⓒa₂ß₂ homotetramer

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 62AP

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Bradykinin is a linear nonapeptide released by blood plasma globulin in response to a wasp sting. It is a very potent pain-causing agent. Its constituent amino acids are 2R, G, 2F, 3P, S. The sue of 2,4-dinitrofluorobenzene and carboxypeptidase shows that both terminal residues are arginine. Partial hydrolysis of bradykinin gives the following di- and tripeptides: FS + PGF +PP + SPF + FR + RP
The catalytic efficiency of many enzymes depends on pH. Chymotrypsinshows a maximum value of kcat/KM at pH 8. Detailed analysis shows thatkcat increases rapidly between pH 6 and 7 and remains constant at higherpH. KM also increases rapidly between pH 8 and 10. Suggest explanationsfor these observations.
I did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.
An enzyme reaction takes place in a 10mL solution that has a total citrate concentration of 120mM and an initial pH of 7.00. During the reaction, 0.2mmoles of acid are produced. (pKa values for citric acid: pKa1=3.15, pKa2=4.77, pKa3=6.40) a) At pH 7.00 (before the enzyme reaction occurs), determine the concentrations of the predominant forms of citrate in solution. b) calculate the pH of the solution after the enzymatic reaction has occurred.
The catalytic efficiency of many enzymes depends on pH. Chymotrypsin, which has a well-known catalytic mechanism, shows a maximum value of kcat/Km at pH 8.0. A) Draw a pH curve of chymotrypsin activity over the pH range of 5 to 10 and briefly explain the rationale within the context of catalysis for your depiction. In particular, note how kcat and Km may change over this pH range. B) Enzymes of the a-amylase family catalyze a reaction by forming a covalent intermediate analogous to chymotrypsin, but to a conserved aspartate residue. Illustrate a catalytic mechanism containing a tetrahedral intermediate for a glycogen debranching enzyme based upon its potential membership in the a-amylase family. (don’t need to draw a whole glycogen)
Relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10-5and 10-8M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 103and 105M, respectively. Which protein has the highest affinity for ligand X? Explain your reasoning.
Given the following peptide SEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in as shown. (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.
Put the following in order of increasing pka and explain ur reasoning
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If the concentration of PB2+, is found to be 1.3*10^-9mol/L in a saturated solution of Pb3(PO4)2, what is the ksp of Pb3(PO4)2?
Tetrapeptide A is completely hydrolysed under acidic conditions to yield alanine, aspartic acid, isoleucine and valine. On neutralisation of the hydrolysate, an odour of ammonia is detected. The reaction of the tetrapeptide with phenylisothiocyanate, followed by mild hydrolysis yields no phenylthiohydantoin derivative. Incubation of A with carboxypeptidase A has no effect either. Explain...
Can u explain the answers pls thank u