Calculate the charge of Alanine at pH 8.5 Calculate the charge of Aspartate at pH 3.65 Calculate the charge of Arginine at pH 12.48 Calculate the charge of Glutamate at pH 7.5 Calculate the charge of Alanine at pH 9.4
please show me how to solve for these three questions below. a) what is the charge due to a glutamyl group in the middle of a protein at pH 1? b) at pH 15, what is the net charge of glutamate? c) at pH 15, what is the net charge of glycerol phosphate?
what would be the net charge of a protein sequence methionine- cysteine- glutamine-leucine-valine- proline- glutamate- asparagine- lysine at ph 1.5, 7 and 12
Calculate [H+] and [OH-] for each solution at 25°C pH= 7.5 pH= 12.3 pH= 2.3 *please write in print (legibly)*
Hemoglobin A has a pI = 6.9. A variant, hemoglobin M, has a residue of glutamate at position 67 instead of valine. What effect does this replacement in electrophoretic behavior at pH 7.5? Thats the only info provided. :(
If the pI for a particular amino acid is 7.5, at which pH will the net charge on the molecule be 1-? 2.5 7.5 5.0 10.0
Draw the predominant form for glutamate in a solution with each pH listed below. Draw the mooecule including charges where needed, do not draw a fischer projection. pH=0 pH=3 pH=6 pH=11
What is the pI of glutamate? pK1= 2.2 pK2=3.5 pKr=8.5 Rule: pH > pKa deprotonated, pH < pKa protonated
Calculate the pH of a 7.5 x 10-5 M NaOH solution. Record your answer in the correct number of significant figures.
Please calculate the following for the buffers below: Phosphate (pH = 7.5) What is the ratio of A-/HA in your buffer after your adjusted its pH to the required value? How many micromoles of A- and HA are present in the solution? If you now add 3mL of 1 NaOH, will you still have a valid buffer? CAS (pH = 10.5) If you now add 3mL of 1 NaOH, will you still have a valid buffer? How many micromoles of...