The role of the cytoskeleton in intracellular signal transduction. Introduction: Cytoskeleton is a microscopic network of protein filaments and tubules in the cytoplasm of living cells. This network gives shape and structure to the cells. Intracellular organization is also controlled by the cytoskeleton. All types of cellular movements, such as chromosomal movements, transport of vesicle, snd cell divisio, nnvolve these filamentous structures.

Question

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.

Answer 1

Question

Chapter 2, Problem 31RQ

Summary Introduction

To review:

The role of the cytoskeleton in intracellular signal transduction.

Introduction:

Cytoskeleton is a microscopic network of protein filaments and tubules in the cytoplasm of living cells. This network gives shape and structure to the cells. Intracellular organization is also controlled by the cytoskeleton. All types of cellular movements, such as chromosomal movements, transport of vesicle, snd cell divisio, nnvolve these filamentous structures.

Expert Solution & Answer

Trending nowThis is a popular solution!

See solution

Check out sample textbook solution

Students have asked these similar questions

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.