Draw the structure of the dipeptide Lys-Glu at pH 7.0. Label the following:
a) Peptide bond
b) N-terminus
c) C-terminus
d) An α-amino group and an ε-amino group
e) An α-carboxylate group and a Y-carboxylate group
Draw the structure of the dipeptide Lys-Glu at pH 7.0. Label the following: a) Peptide bond...
Draw the Lewis structure of the pentapeptide Met-Glu-Leu-His-Lys as it will exist at the following pH's РH 2.5 a. b. рH 7.0 pH 10.0 с. d. What is the isoelectric point for this peptide? Draw the Lewis structure of the pentapeptide Met-Glu-Leu-His-Lys as it will exist at the following pH's РH 2.5 a. b. рH 7.0 pH 10.0 с. d. What is the isoelectric point for this peptide?
1. Draw the dipeptide His-Gly at pH 7.4. 2. Label the amino terminus, the carboxy terminus, the two alpha carbons, and the peptide bond (1pt). 3. Calculate it’s net charge. 4. What is the net charge of this dipeptide at pH = 2? 5. List the levels of protein structure and the types of bonds/interactions that are characteristic of each level.
A) Draw the dipeptide R-T at pH 7 and CLEARLY label the peptide bond to be broken in the presence of trypsin. 3pts B) Draw the five-step mechanism for the trypsin cleavage of the dipeptide. 5pts C) Label the transition state each time it is formed. 1pt D) What mechanism is used to describe this bisubstrate reaction? 1 pt
9 (a) In the box below, draw the dipeptide Phe-Arg at pH 7, with the N-terminus at the left and the C-terminus on the right. 9 (b) Draw a single box around the three non-hydrogen atoms directly involved in the peptide bond. 9 (c) Label the Phi (φ) and Psi (ψ) torsion angles in your drawing. 9 (d) How many positive charges are on this dipeptide at pH 7? 9 (e) What is the total net charge at pH 7...
On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together. If the two amino acids are valine and threonine, predict the overall charge of the dipeptide at pH 7. Do not forget to consider the amino (N-terminal) and carboxy (C-terminal) of the dipeptide, as well as the R groups. Select one: a. +2 b. -2 c. 0 d. -1 e. +1
Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser. Problem 24-44 ConstantsI Periodic Table Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, lle, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala and the C terminus is lle. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that...
Draw the structure of the peptide Arg-Met-His-Val-Glu, label the coplanar atoms in one peptide bond and estimate a pI.
Calculate the pI for this peptide. Gly Asp Lys Cys Glu His Met Table 1. Group pka c-teminus 3.5 his 6.0 n-terminus 9.0 lys 10.5 asp/glu 4.0 cys 8.4 tyr 10.5 arg 12.5
Sketch the structure of the tetrapeptide Ser-Phe-Asp-Lys. Clearly show the R groups, all the peptide bonds, the peptide planes, the N-terminus, the C-terminus, and approximate charges on all ionic groups at a pH of 7.0.
6. A peptide has the sequence Cys-His-Phe-Glu-Ala-Arg a. Write the single letter sequence of the peptide b. Calculate the percentage and indicate the charge of the predominant peptide species at pH 6.5. Use the following pKa values: pKa Cys = 8.3, pKa N-terminus = 10.8, pKa His =6.0, pKa Glu = 4.3, pKa Arg = 12.5, pKa C-terminus =2.0 c. What is the charge of the peptide at pH 4.3? d. Draw the chemical structure of the predominant peptide species...