Question

a) Draw the tetrapeptide Cys-Pro-Leu-Asp at pH=1 b) Assuming pka of the side chain of cysteine...

a) Draw the tetrapeptide Cys-Pro-Leu-Asp at pH=1

b) Assuming pka of the side chain of cysteine is 8.5, what is the pI of this tetrapeptide?

Homework Answers

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
For the peptide Ala-His-Glu-Val-Asp-Cys-Lys-Leu what is the net charge at pH 3? Please explain how you...
For the peptide Ala-His-Glu-Val-Asp-Cys-Lys-Leu what is the net charge at pH 3? Please explain how you get the charge of each amino acid.
For the following amino acid strand (shown from N to C-terminus) Asp-Pro-Cys-Gly-Ser-Try A.) Draw the structure...
For the following amino acid strand (shown from N to C-terminus) Asp-Pro-Cys-Gly-Ser-Try A.) Draw the structure of the hexapeptide w/ appropriate stereochemistry.    B.) What forces hold the above peptide in an α-helix? What part of the peptide is involved? C.) This hexapeptide is one of three peptide chains in a protein. What forces hold the above peptide in its 4o structure?
1. The OH group on the side chain of Tyr (pKa= 10.9) is more acidic than...
1. The OH group on the side chain of Tyr (pKa= 10.9) is more acidic than the OH groups on the side chains of Ser and Thr. Suggest as many possible explanations for the following facts. Hint; Conder resonance. 2. The NH2 group on the side chain of lysine is much more basic than the NH2 group on the side chains of Asp and Gln. Suggest as many possible explanations for the following facts. Hint; Conder resonance.
1. Based on pKa values, which amino acid side chains are easiest to protonate and deprotonate...
1. Based on pKa values, which amino acid side chains are easiest to protonate and deprotonate at cellular pH (7.4)? (Choose all that apply) Aspartic Acid Histidine Lysine Serine Arginine Glutamic Acid Cysteine Tyrosine 2. At pH 7.4, which of the amino acid sidechains or R-groups below will be mostly deprotonated? (Chose all that apply) Glutamatic Acid Aspartic Acid Arginine   Tyrosine Serine   Lysine   Histidine Cysteine 3. Acetyltransferase enzymes modify a lysine side chain with an acetyl group. Titration of the...
(a) Calculate the PI of the peptide below: Met-His-Leu-Pro-Asn-Glu b) Which method would you use to...
(a) Calculate the PI of the peptide below: Met-His-Leu-Pro-Asn-Glu b) Which method would you use to purify the peptide in question 1: Gel filtration chromatography, or ion exchange chromatography? Why? What resin would you use?
What would be the charge of this peptide, Asn-Arg-Met-Lys-His-Pro-Trp-His-Thr-Tyr-Ser-Gly-Glu-Leu-Val-Trp, at a pH of 1 and a...
What would be the charge of this peptide, Asn-Arg-Met-Lys-His-Pro-Trp-His-Thr-Tyr-Ser-Gly-Glu-Leu-Val-Trp, at a pH of 1 and a pH of 11?
1.     The primary sequence of the peptide listed below. H2N - Asp-Thr-Phe-Lys-COOH H2N – D -T...
1.     The primary sequence of the peptide listed below. H2N - Asp-Thr-Phe-Lys-COOH H2N – D -T – F – K – COOH Use the one letter amino acid code and identify from N-terminus to C-terminus. a.     Determine the pI of the peptide. (Round to 2 decimal points) b.     Would mutating residue #3 to Ala change the pI of the peptide? Explain. c.      Which type of noncovalent interaction would the indicated residue side chain make at the given pH? (H-bond, Hydrophobic...