Question
In: Chemistry
Indicate how the pKa of the ionizable group of histidine would be changed in a nonpolar...
Indicate how the pKa of the ionizable group of histidine would be changed in a nonpolar pocket (increase/decrease) PLEASE EXPLAIN WHY. I thought it would increase but that's not correct
Solutions
Expert Solution
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queen_honey_blossom answered 1 year agoRelated Solutions
Histidine has ionizable groups with pKa values of 1.8, 6.0, and 9.2, as shown below. A...
Histidine has ionizable groups with pKa values of 1.8, 6.0, and
9.2, as shown below. A biochemist makes up 100 mL of a 0.100 M
solution of histidine at a pH of 5.40. She then adds 40 mL of 0.10
M HCl. What is the pH of the resulting solution?
The book answer is 2.4. Please show work to help me understand how
they arrived at this.
A molecule has an ionizable group with a pKa value of 8. At pH equal to...
A molecule has an ionizable group with a pKa
value of 8. At pH equal to 7.0, estimate roughly how much of the
group is deprotonated (expressed as %)? Use 2 decimal points. Do
not use scientific notation to enter your answer.
All amino acids have two ionizable functional groups: an α-amino group (average pKa of 9.4) and...
All amino acids have two ionizable functional groups: an α-amino
group (average pKa of 9.4) and an α-carboxylic acid group (average
pKa of 2.2). Arginine also has an ionizable side chain (R group)
with a pKa of ~12.5. One of the possible ionization states of
arginine is shown below.
At what pH would the above structure be the predominant
ionization state? Note: Consider the ionization state of all three
of the functional groups.
The protonated form of the R group...
is the pka of a histidine side chain always the same as that of the free...
is the pka of a histidine side chain always the same as that of
the free amino acid? Why?
how do titration curves differ between non ionizable and
ionizable r groups? why?
Biochemistry
A nonstandard amino acid has three ionizable groups, with pKa values of 2.6, 7.4, and 10.13....
A nonstandard amino acid has three ionizable groups, with pKa
values of 2.6, 7.4, and 10.13. A 0.1 M solution of this amino acid
is made, 100 ml total, at pH 2.6. To this solution is added 10 ml
of 1 M NaOH. What is the final pH of this solution after the
addition?
A) 3.2
B) 8.0
C) 7.4
D) 6.8
E) 10.13
The pKa of the α-carboxyl group of phenylalanine is 1.83, and the pKa of its α-amino...
The pKa of the α-carboxyl group of phenylalanine is 1.83, and
the pKa of its α-amino group is 9.13. Calculate the average net
charge on phenylalanine if it is in a solution that has a pH of
8.30. If the charge is positive, do not enter a + sign.
The pKa of the α-carboxyl group of phenylalanine is 1.83, and the pKa of its α-amino...
The pKa of the α-carboxyl group of phenylalanine is 1.83, and
the pKa of its α-amino group is is 9.13.
Calculate the average net charge
on phenylalanine if it is in a solution that has a pH of 8.00 (If
the charge is positive, you do not need to enter a " +"
sign.)
Please show your work.
The pKa of the α-carboxyl group of phenylalanine is 1.83, and the pKa of its α-amino...
The pKa of the α-carboxyl group of phenylalanine is 1.83, and
the pKa of its α-amino group is 9.13. Calculate the average net
charge on phenylalanine if it is in a solution that has a pH of
8.20. If the charge is positive, do not enter a + sign.
How is Histidine used to modulate protein activity?
How is Histidine used to modulate protein activity?
Draw the structure of protonated histidine and indicate (draw and name) all possible non bonding interactions...
Draw the structure of protonated histidine and indicate (draw
and name) all possible non bonding interactions with water. include
H bonding, and Hydration Spheres
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