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Q: What is the net charge of phosphatidylserine in physiological pH?
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What is the net charge of phosphatidylserine at pH 6.0?

- 1


What is the net charge of the dipeptide glu-lys at physiological pH?

Lys is basic and has a + charge, glu is acidic and - charged = net charge 0


Net charge of histidine in pH 1 3 5 11?

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


What is the net charge of phosphatidylserine at pH 7?

DNA molecules are connected via a 5'-3' phosphodiester linkage to ribose molecules. The phosphate group within this linkage is contains a negatively charged oxygen atom at a PH of 7. This gives DNA its charge.


What is the net charge for lysine?

Depends on the pH. The lysine nitrogen is positively charged until pH 9.0 (so at physiological pH it is positively charged). See http://usm.maine.edu/~newton/Chy251_253/Lectures/AminoAcids/AminoAcids2.html near the bottom.


The pI of a lysozyme is 11. What is the pH range in which the overall charge of the lysozyme is positive?

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.


PH of physiological saline?

No specific pH


At Ph 10 what charge would Zwitterion ion have?

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.


What charge does phenylalanine have at pH of 7.0?

Phenylalanine has a net 0 charge at pH 7.0 as the carboxy end has been deprotonated and the amino end still contains it's proton (hydrogen).


What amino acid would work best as a buffer close to physiological pH?

Histidine is the amino acid that function at the physiological PH. The reason being that the Pka value of his is 6.8 close to the physiological PH of the blood i.e. 7.4


What is meant by isoelectric point of protein?

It is the pH at which a particular molecule or surface carries no net electrical charge


How pH affect ionic bonding?

At low pH the over all net charge, for example amino acid residue ( which is connected by by ionic bonding) is going to be protonated which means there will be no ionic bonding at very low pH. As you raise the pH depending on the given pKas part of the residue starts to deprotonate which also could alter the net charge i.e the the ionic bonding is going to be affected.