At pH 10, guanine is primarily in its neutral form, as the pKa values of its functional groups suggest that at this pH, the amino group is protonated, while the keto group is deprotonated. The overall charge of guanine at this pH is typically neutral, as the positive and negative charges balance each other out. However, the specific charge state can vary slightly depending on the local environment and interactions.
At pH 6.0, the net charge of phosphatidylserine is -1. This is because the phosphate head group is negatively charged and would be deprotonated at this pH, contributing a net charge of -1 to the molecule.
At pH 5.7, serine would have a positive charge. This is because the pKa of serine's side chain is around 9.21, so at pH below its pKa, the side chain will be protonated, resulting in a positive charge.
if the pH is 4.7, the H+ concentration is 2 x 10-5
[H+] = 1 x 10-10 M then pH = 10
Guanine is a polar molecule due to the presence of electronegative atoms (oxygen and nitrogen) in its structure. This results in an uneven distribution of charge, making it attract other polar molecules through dipole-dipole interactions.
The relationship between pH and pI is that the pH of a solution can affect the charge of a protein, while the pI (isoelectric point) is the pH at which a protein has no net charge. At a pH below the pI, the protein will have a net positive charge, and at a pH above the pI, the protein will have a net negative charge.
In a neutral pH environment, the charge of lysine is positive.
At pH 7, ATP has a net charge of -4.
it would depend on amino acid in question. pH above amino acid pI, zwitterion will carry net negative (-) charge. at pH below pI, zwitterion will carry net positive (+) charge. depending on the amino acid, some have more than one acidic or basic functional group. such functional groups can make the amino acid vary in net charge from 2- to 2+ if not more.
At pH values less than the pI point the net charge is positive. If at pH above the pI poiint, the charge will be negative.
The charge on the lysine molecule is positive when it is in a solution with a pH of 7.
The pH depends on the concentration (how much is dissolved in a given volume of water) Since it is a strong monoprotic acid the pH equals the negative logarithm of its molar concentration. A 1M solution has a pH of 0 a .1M solution has a pH of 1 and so on until a pH of about 7.
pK1 = 2.3, pKr = 6, pK2 = 9.7 (all approximate) at physiological pH, histidine has no net charge. at pH 1, below all pKas and charge is +2 at pH 3, amine group proton pops off, so +1 charge at pH 5, still below 6 and above 2.3 so +1 charge if had pH above 6, for instance... at pH of 8 net charge is zero, or neutral... such that it is neutral at physiological pH (a bit above a pH of 7) at pH 11, exceeds all pKas of amine, acid group, and R group. So net charge of -1 amine deprotonation, carboxylic acid deprotonation, and R group deprotonation happen pH 11 because it exceeds all pKs
At pH 6.0, the net charge of phosphatidylserine is -1. This is because the phosphate head group is negatively charged and would be deprotonated at this pH, contributing a net charge of -1 to the molecule.
The isoelectric point of a molecule can be determined by finding the pH at which the molecule carries no net electrical charge. This can be done by plotting the molecule's charge as a function of pH and identifying the pH at which the charge is zero.
A pH of 10 is considered basic, or alkaline, on the pH scale. Substances with a pH above 7 are classified as bases.
The pH of the solution is 10. The pH is calculated as the negative base 10 logarithm of the hydronium ion concentration. pH = -log[H3O+]. In this case, pH = -log(1.00 x 10^-10) = 10.