The reason for use of alpha helices in the membrane-spanning for the G-protein-coupled receptors needs to be explained. Concept Introduction : The structure of alpha-helix is a polypeptide chain like a coiled rod giving a spring like structure. These polypeptide chains are bonded together with hydrogen bonds. The beta strands are responsible for bonding in beta-pleated sheets where they linked in lateral manner with hydrogen bonds resulting formation of a backbone. The number of amino acids involved in beta strand or chain formation is from 3-10.

Question

Disulfide bond formation is a regularly observed protien modification that occurs in the lumen of the ER. Explain why disulfifde bond formation is a modification only found in secretory proteins and the extracellular domain of plasma membrane proteins. Furthermore, highlight the advantages disulfide bonds provide to these proteins.

Answer 1

Question

Chapter 32, Problem 11P

Interpretation Introduction

Interpretation:

The reason for use of alpha helices in the membrane-spanning for the G-protein-coupled receptors needs to be explained.

Concept Introduction :

The structure of alpha-helix is a polypeptide chain like a coiled rod giving a spring like structure. These polypeptide chains are bonded together with hydrogen bonds. The beta strands are responsible for bonding in beta-pleated sheets where they linked in lateral manner with hydrogen bonds resulting formation of a backbone. The number of amino acids involved in beta strand or chain formation is from 3-10.

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