How the study of LDL receptor binding by a human rhinovirus HRV2, provided support for model of LDL particle displacement should be discussed. Concept Introduction: LDL receptor has five domains. N terminal LDL binding domain contains seven cysteine rich repeats referred as R1 to R7. Next epidermal growth factor repeats and ß propeller module can be found. Those segments are followed by O-linked oligosaccharide, a membrane spanning segment and another segment extended towards the cytosol. LDL particles bind with R4 and R5 cysteine repeats. At low pH, the LDL receptor polypeptide folds so that ß propeller domain is associated with R4 and R5 displacing the LDL particle. These two repeats contain two loops connected by 3 disulfide bonds. Second loop of each repeat have Asp and Glu acidic residues and acts as a Ca 2+ binding site.

Question

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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Question

Chapter 24, Problem 18P

Interpretation Introduction

Interpretation:

How the study of LDL receptor binding by a human rhinovirus HRV2, provided support for model of LDL particle displacement should be discussed.

Concept Introduction:

LDL receptor has five domains. N terminal LDL binding domain contains seven cysteine rich repeats referred as R1 to R7. Next epidermal growth factor repeats and ß propeller module can be found. Those segments are followed by O-linked oligosaccharide, a membrane spanning segment and another segment extended towards the cytosol. LDL particles bind with R4 and R5 cysteine repeats. At low pH, the LDL receptor polypeptide folds so that ß propeller domain is associated with R4 and R5 displacing the LDL particle. These two repeats contain two loops connected by 3 disulfide bonds. Second loop of each repeat have Asp and Glu acidic residues and acts as a Ca²⁺ binding site.

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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.

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