Hey, im 1st year med student and we have this buffers and pH tutorial i need to do and its background work, using the Henderson Hasselbalch equation is simple but these two questions im struggling with. Will rep anyone that can help explain the answers.
1) Write down your prediction of the structure of the predominant ionic species of the dipeptide aspartyl cysteine at each of the following pH values : 1,5,7,9,11
predominant ionic species = no idea!
2)a) What causes the pKa for the side chain of histidine residues in a protein to differ from the value for the simple amino acid?
I put neighbouring amino acid side chains in the haemoglobin molecule?
b) How could the pKa values change, as haemoglobin molecules are oxygenated or deoxygenated?
pKa is the pH at which acid is half dissociated so does oxygen affect that?
c) What is the physiological consequence of this difference in pKa values?
Gives the haemoglobin a wider range for working effectively as a buffer?
Thanks in advance