The following is the titration curve of Cysteine. Different charge states of Cys are shown inthe table below. Answer the following questions using the information given here.BAQuestion 6ů98Hd20210€ 5201Form 4Form 310O=O-0--8--20(OH) (equivalents)H&N=CH-C-0Form 2--1-6-505H₂N-CH-C-OHForm 1-6-5SHSH. Which is the most predominant form(s) of Cysteine at the point A on the titration curve?[Select]• Identify which form (among the given above) would Cys assume when the solutions's pH isat its pl[Select]and• Identify the pl (isoelectric point) of this amino acid on the graph: it is marked as[Select]on the graph.Question 7

Answered: Image /qna-images/answer/9cfb7197-7d90-43fe-ba94-df29c85823ea.jpg

5-60 SH SH . Which is the most predominant form(s) of Cysteine at the point A on the titration curve? [Select] • Identify which form (among the given above) would Cys assume when the solutions's pH is at its pl [Select] and • Identify the pl (isoelectric point) of this amino acid on the graph: it is marked as [Select] on the graph.

5-60 SH SH . Which is the most predominant form(s) of Cysteine at the point A on the titration curve? [Select] • Identify which form (among the given above) would Cys assume when the solutions's pH is at its pl [Select] and • Identify the pl (isoelectric point) of this amino acid on the graph: it is marked as [Select] on the graph.

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 50AP: The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in...

See similar textbooks

Similar questions

The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in the chain. Why is proline never present in a protein helix?
How can distance validate non-covalent interactions? Also, please explain if the distance between c-alpha of a particular residue in an enzyme and c-alpha of its ligand are 12.4 Å, 11.7 Å, 6.5 Å, 7.6 Å, and 7.7 Å, what does that mean? What is the meaningful distance, what is the legth of hydrophobic,hydrophilic, h-bond...?
At what pH is the formationof the acyl-enzyme complex most likely to occur. provide a point. Provide an explanation for this.
please explain What percentage of a side-chain sulfhydryl group of cysteine is protonated at pH 7.9?
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?
Which of the following best represents the structure of an amino acid in basic solution (pH=11)?
Which of the following is an acceptable name for the peptide sequence below?
draw the electronic configuration of platinium IIII in ormaplatine (complex and expect the followings: a. the charge of this drug b. the shape of its complex. c. the expected type of hybridization d. the number of coordination covalent bonds in this drug e. what is the pharmacological use of ormaplatinePlease explain the point (d) and how I can calculate it
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.
The Kb for dimethylamine, CH3NH2, at 25oC is 4.0×10-4. What’s the Ka of its conjugate acid?
What is known as Ziegler–Natta catalysts ?
Given the normal blood pH is 7.35, what is the expected pKa of H2CO3 ([H2CO3] = 0.50M and [HCO3-] = 0.100M) ?