2. Using the standard 3.6 amino acids per turn (360°) and the helical wheel below, plot eachsequence on a helical wheel. Circle the hydrophobic residues and draw a square aroundthe hydrophilic residues.Clearly indicate which of the 4 sequences creates an amphipathic helix where one side isburied on the inside of the protein and the other is exposed to water. Explain why thepeptide you chose is the correct one and why the other 3 are incorrect.CRAAPNRKIVLETYSIEPDANFRACISLWEKATVEMAVRNSARAIMEILKVDAQFN

Helical wheel plot is used to alpha helix of protein structure in 2D plane. This is helpful in…

Answered: 2. Using the standard 3.6 amino acids…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

What can we most-accurately say about the polypeptide with the primary sequence KNEADING? a.It has two acidic R groups b.It has three basic R groups c. It has two nonpolar neutral R groups d. It contains three polar neutral R groups e. It contains a disulfide linkage
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
17. How would you computationally predict the thermodynamic stability of a long, extended RNA helix? Please explain in 1 sentence how structural "favorability" can be predicted
(A) Give the polypeptide translation of the RNA sequence below. 5’-AUGGAAAUCAAAGUCAACCUUGAGUUUAGA-3’ (B) Write the chemical structure of the polypeptide sequence you determined in part (a) (C) Given the chemical structure of the polypeptide sequence you have written in part (b), answer True or False for each of the 5 statements below. (1) At least one of the amino acids in the sequence can undergo phosphorylation (2) The sequence looks like it could form a β turn (3) The sequence looks like it could form a β strand with one surface facing the interior of the protein and the other surface exposed to water (4) At least one of the amino acids in the polypeptide sequence can undergo oxidation to form a disulfide bridge to another polypeptide (5) The sequence looks like it could form an α helix that would be part of a coiled coil structure within a protein
1 point Before we start the actual translation process. If we look at our transcript from sequence I, we can predict how long the polypeptide will be. 544545-33454454 Find the Open reading frame. Then tell me how many amino acids are in this poly-peptide? Provide a single integer Type your answer... A8885-349953-
2. Of the two sequences, which is more likely to have helical structure. Explain. a) -Glu-Asp-Glu-Glu-Asp-Leu- b) -Glu-Leu-Asp-Arg-Val-Lys-

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