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

Biochemistry Question. Please help solve. Thank you! Based upon knowledge of oxidation of bioorganic compounds and howmuch energy is released during their oxidation, rank the following, from most to least, with respect to how much energy would be produced from each during their oxidation. Explain your placement for each one.

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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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