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Why does the Asp-His ion pair contribute more energy at pH 6.0 than at low or high pH? At pH 10.0, Asp is protonated and His may be deprotonated. At pH 6.0, Asp is protonated and His may be deprotonated. At pH 2.0, Asp and His are both deprotonated. At pH 10.0, Asp and His are both protonated. At pH 6.0, Asp is deprotonated and His may be protonated.

Why does the Asp-His ion pair contribute more energy at pH 6.0 than at low or high pH? At pH 10.0, Asp is protonated and His may be deprotonated. At pH 6.0, Asp is protonated and His may be deprotonated. At pH 2.0, Asp and His are both deprotonated. At pH 10.0, Asp and His are both protonated. At pH 6.0, Asp is deprotonated and His may be protonated.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Like ribonuclease A, lysozyme from T4 phage is a model enzyme for understanding the energetics and pathways of protein folding. Unlike ribonuclease A, T4 lysozyme does not contain any disulfide bonds. A number of studies have quantified the thermodynamic contributions individual amino acid residues and their interactions make to lysozyme folding. An ion pair between an Asp residue and a His residue in lysozyme contributes 13-21 kJ/mol of favorable folding energy at pH 6.0. However, this ion pair contributes much less to lysozyme folding at either pH 2.0 or pH 10.0. Why does the Asp-His ion pair contribute more energy at pH 6.0 than at low or high pH? At pH 10.0, Asp is protonated and His may be deprotonated. At pH 6.0, Asp is protonated and His may be deprotonated. At pH 2.0, Asp and His are both deprotonated. At pH 10.0, Asp and His are both protonated. ● At pH 6.0, Asp is deprotonated and His may be protonated.
Transcribed Image Text:Like ribonuclease A, lysozyme from T4 phage is a model enzyme for understanding the energetics and pathways of protein folding. Unlike ribonuclease A, T4 lysozyme does not contain any disulfide bonds. A number of studies have quantified the thermodynamic contributions individual amino acid residues and their interactions make to lysozyme folding. An ion pair between an Asp residue and a His residue in lysozyme contributes 13-21 kJ/mol of favorable folding energy at pH 6.0. However, this ion pair contributes much less to lysozyme folding at either pH 2.0 or pH 10.0. Why does the Asp-His ion pair contribute more energy at pH 6.0 than at low or high pH? At pH 10.0, Asp is protonated and His may be deprotonated. At pH 6.0, Asp is protonated and His may be deprotonated. At pH 2.0, Asp and His are both deprotonated. At pH 10.0, Asp and His are both protonated. ● At pH 6.0, Asp is deprotonated and His may be protonated.
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