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#pH 7

5 public questions tagged with this topic.

Which property causes glutamic acid to move towards anode at pH 7?

Amino acid migration during electrophoresis depends on net charge dictated by relationship between buffer pH and isoelectric point. Glutamic acid possesses acidic side chain with pI approximately 3.22 due to two carboxyl groups. At pH 7, well above pI, both alpha and side-chain carboxyls are deprotonated, conferring net negative charge of minus one to minus two. Anions migrate toward positively charged anode under electric field. Basic pI would imply cationic state and cathodal migration, while molecular weight and solubility do not determine direction. Thus acidic pI explains anodal movement of glutamic acid at neutral pH.

Ref: NCERT Biology Class XII Principles on Klenow fill-in labeling, Lehninger Chapter 9 DNA cloning techniques, and Molecular Cloning by Sambrook Chapter 10 documenting end-labeling of cohesive termini.

Elutes first in cation exchange at pH 7?

Cation exchange matrix bears negative functional groups attracting positively charged species. At pH 7, acidic amino acids like aspartate with pI around 3 are deprotonated and negatively charged, thus repelled and eluted first without binding. Basic residues like lysine remain positively charged and bind strongly. Neutral aliphatic residues such as valine and leucine carry little net charge at neutral pH, resulting in minimal interaction. Hence in a mixture, aspartate exits earliest, allowing charge-based fractionation. Adjusting pH relative to amino acid pI values facilitates predictable elution order for purification of peptides and proteins.

Ref: NCERT Biology Class XII Principles on Klenow fill-in labeling, Lehninger Chapter 9 DNA cloning techniques, and Molecular Cloning by Sambrook Chapter 10 documenting end-labeling of cohesive termini.

Which of the following amino acids contributes most to a peptide’s negative charge at pH 7?

Aspartic acid is the scientifically accurate answer to this question. Within the study of Titration of Amino Acids, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of Aspartic acid directly address what is being asked. Among the other options, Lysine, Arginine, and Histidine do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 3