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17 Nov 2019

Using the Henderson-Hasselbach equation

1. Calculate the charge of glutamic acid and aspartic side chain at pH 2.5 and pH 11.5. (pKa are 4.2 and 3.9 respectively)

2. Calculate the charge of tyrosine and arginie side chain at pH 3.5 and pH 9.5. (pKa10.1 and 12.5 respectively)

PLEASE SHOW THE CALCULATION ON HOW THE CHARGE WAS OBTAINED. THANKS!! This is a biochemistry question

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Collen VonLv2

16 Apr 2019

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Using the Henderson-Hasselbach equation

1. Calculate the charge of Cysteine side chain at pH 1.5 and pH 10.5. (pKa of Cysteine side chain is 8.4)

2. Calculate the charge of Histidine side chain at pH 1.5 and pH 10.5. (pKa of Cysteine side chain is 6)

PLEASE SHOW THE CALCULATION ON HOW THE CHARGE WAS OBTAINED. THANKS!!

This is a biochemistry question

Using the Henderson-Hasselbach equation calculate the charge on these amino acids the various pH's in the table

	Cys	His	Glu	Asp	Tyr	Arg	Lys
1.5
2.5
3.5
4.5
5.5
6.5
7.5
8.5
9.5
10.5
11.5
12.5

Please show the calculation if you can. And this is a biochemistry question

A histidine residue in a protein has a side chain pKa of 6.3. Due to a conformational shift, an amino acid move into the close proximity of this histidine, shifting the histidine pKa to 5.7.

if the protein has the above histidine in it was in a solution of pH 6.5, what is the change in the net charge of this histidine (show all the calculation)?

what is the likely identity of the residue that causes the pKa shift for the above histidine residue? If there is more than one possible candidate, then list them all. Explain why these candidates cause the shift in the histidine pKa.

Extra Info:

equations: Vo = {Vmax [S]} / {Km + [S]}; pH = pKa + log {[base]/[acid]}; ÎG = ÎH - TÎS

pKa of the side chain R-groups are: D (3.9), E (4.2), H (6.0)' C (8.3), Y (10.1), K (10.5), and R (12.5).

pKa of amino acid Î±-amino group (9.60) and Î±-carboxyl group (2.10).

pKa of N-terminal oligopeptide a-mino group (7.40) and C-terminal a-carboxyl group (3.6)

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