WORLD OF CELL+MASTERING ACCESS >CUSTOM
WORLD OF CELL+MASTERING ACCESS >CUSTOM
9th Edition
ISBN: 9781323445044
Author: Hardin
Publisher: PEARSON C
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Chapter 19, Problem 19.9PS

(a)

Summary Introduction

To determine: The maintenance and establishment of high concentration of Binding protein (BiP) in the lumen of endoplasmic reticulum and lesser concentrations in other regions of the cells.

Introduction: Protein folding is a process where folding of the polypeptide chain to form a 3D structure of protein takes place. Many different types of molecular interactions are involved in the process.

(b)

Summary Introduction

To determine: The effect on the cell if the gene encoding BiP acquires a mutation that disrupts the protein binding site for hydrophobic amino acids.

Introduction: Protein folding is a process where folding of the polypeptide chain to form a 3D structure of protein takes place. Many different types of molecular interactions are involved in the process.

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Reposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?
resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?
Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartate
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