Biochemistry, The Molecular Basis of Life, 6th Edition
Biochemistry, The Molecular Basis of Life, 6th Edition
6th Edition
ISBN: 9780190259204
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 2, Problem 40RQ
Summary Introduction

To review:

The difference between Endoplasmic Reticulum (ER) stress, unfolded protein response, and ER-associated protein degradation.

Introduction:

ER stress, unfolded protein response, and ER-associated protein degradation are all related processes as they deal with abnormally folded proteins. One process leads to initiation of another process.

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A protein biochemist attempted to determine the amino acid sequence of a decapeptide. The results from the trypsin, chymotrypsin, and cyanogen bromide treatments are shown: ⚫ Trypsin digestion gave two fragments with multiple residues (not in order): • T1: Ala, Arg, Phe, Gly, Thr, Trp, Tyr o T2: Lys, Met, Val Chymotrypsin digestion gave four fragments with multiple residues (not in order): • CT1: Ala, Phe • CT2: Thr, Trp • CT3: Lys, Met, Tyr, Val 。 CT4: Arg, Gly ⚫ Treatment with cyanogen bromide yielded a single amino acid, methionine, and a nonapeptide. What is a possible sequence of the decapeptide? Use three-letter abbreviations in your answer, and add a dash between each residue.
A protein biochemist attempted to determine the amino acid sequence of a decapeptide. The results from the trypsin, chymotrypsin, and cyanogen bromide treatments are shown: • Trypsin digestion gave two fragments with multiple residues (not in order): T1: Ala, Arg, Phe, Gly, Thr, Trp, Tyr • T2: Lys, Met, Val Chymotrypsin digestion gave four fragments with multiple residues (not in order): • CTI: Ala, Phe 。 CT2: Thr, Trp • CT3: Lys, Met, Tyr, Val 。 CT4: Arg, Gly ⚫ Treatment with cyanogen bromide yielded a single amino acid, methionine, and a nonapeptide. What is a possible sequence of the decapeptide? Use three-letter abbreviations in your answer, and add a dash between each residue.
Poly-L-leucine in an organic solvent such as dioxane is a helical, whereas poly-L-isoleucine is not. Why do these amino acids with the same number and kinds of atoms have different helix-forming tendencies? L-isoleucine's methyl group sterically interferes with α-helix formation, whereas L-leucine's methyl group does not interfere. L-isoleucine lacks an NH group that can donate a hydrogen bond to stabilize an a helix, whereas L-leucine has an NH group. L-isoleucine contains a hydrogen-bond acceptor in close proximity to the main chain, whereas L-leucine lacks this group. L-isoleucine's ring structure prevents it from assuming the op value to fit into an a helix, whereas L-isoleucine does not have a ring structure.
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