Using octahedral symmetry, match each ligand SALC with its most likely interaction with a meta within the Lewis acid/base model.

An engineered ligand binds its target with 5 nM affinity at high pH. However, protonation of a histidine residue in the binding site of the ligand renders it unable to bind. Plot the ligand:target complex concentration versus the initial ligand concentration (in protonated or unprotonated form) at pH 4, 5, 6, 7, or 8 (five lines on one plot). Use a total target concentration of 10 nM.

the overall, net ionic charge on this peptide at pH = 7 would be: Cys - Ala - Glu-Arg - Met - Ser

A protein has a dissociation equilibrium constant equal to 4.0um. What is the concentration of free ligand when the fraction of bound sites is 0.7

A HEPTAPEPTIDE that punctures the bacterial cell wall has just been recently isolated from the venom gland of a frog. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrezine Acid Hydrolysis (6 N HC) at 10 C Heptapeptide (2) Arg. Pro, Phe, Tyr, Ala, Lys 2,4 dinitrafluerobenzene DNP-Phe Lys and modified free amino acids Peptide 1 (Ala, Lys) Cleovage with Trypsin, then chrometogrophy Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Peptide 4 (Arg. Tyr) Clevege with Chymetrypsin, then cromategrphy Peptide 5 (Lys, Pro, Ala, Arg)

Please draw the structure of the amino acid Histidine at each ionization state and please also give their net charges.

calculate the net charge of your peptide at I) pH 2.0; ii) pH 6.0 iii) pH 7.0; iv) pH 11.5. show full working and include justification as to how you determined the charge of WEIJIN peptide