How to draw titration of amino acids ？what happen when ph increase from low to high？ 1. what does it means when pka and ph are equal？ 2. Did I calculate p1 correctly？？ 3. Does cysteine lose H in SH ？should it be positively charged or negatively charged after lose H and why？？

Please help, with explanation need. Thank uu

б. Draw all possible products of a single hydrolysis being completed on the following polypeptide: Ala-Ser-Met-Ser

What is the charge on the following peptide at standard biochemical pH? S-Y-D-F-K-I-V-F-L-L +2 -1 0 0 0-2 O +1

a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).

80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.

Some terms will not be used. The prosthetic group of hemoglobin and myoglobin is The organic ring component of heme is Under normal conditions, the central atom of heme is In the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring system. The central atom has bonds: to nitrogen atoms in the porphyrin, one to a residue, and one to oxygen. Answer Bank Fe3+ three heme serine deoxyhemoglobin four Fe2+ oxyhemoglobin рoгphyrin histidine six cysteine

Please be clear in your explanations. This is a practice assignment for an upcoming exam and I'm trying to learn everything.

0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.

Help me please