4. A polypeptide comprised of 17 amino acid res-idues with the sequence on the right is ob-servedby spectroscopic methods to undergo transitionsfrom an a-helix conformation to a B-sheet as afunction of pH and concentration. The acetyl and carboxamide groups are attached covalently to deri-vatize the N- and C-terminal residues, respectively, to avoid charge effects of the end groups.CH3CO-ΤAΤΚΑE LLAKYEATΗK-CONH2(a) (amino acid residues.Write the sequence of this polypeptide with corresponding 3-letter abbreviations for the(b) At pH < 4 the polypeptide forms an a-helix. (i) (the helix? and (ii) (: ·with respect to the positive and negative ends of the macrodipole?) What is the direction of the macrodipole of| Are the charges on the N- and C-terminal residues stabilizing or de-stabilizing(c) (*stabilize the helical conformation. What are the most likely protonation states of the side-chains thatprovide a-helix stabilizing interactions?Use the helical wheel (at the back of the problem set) to identify side chain interactions that

The peptide sequence using 3 letter amino acid code is given below.…

Answered: 4. A polypeptide comprised of 17 amino…

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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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.…
please match all of them
1. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Tyr-Trp-Phe-Cys-Gly - What is observed when the protein sample is subjected to lead sulfide test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result
You are presented with Cytidine 5' triphosphate and Thymidine 5' triphosphate. Draw and upload to Efundi these phosphorylated structures as they would be connected in a polinucleotide in the order CpT / Show the individual phosphorylated structures first then show how they combine to form the polynuleotide. Show at any one of these structures where the glycosidic bond occurs
Antiparallel B sheet 寧 ; Ala side chains Gly side chains Figure 4-14a Lehninger Principles of Biochemistry, Seventh Edition 2017 W. H. Freeman and Company The structure of spider silk is shown above. Mutating the alanine residues to arginine is expected to disrupt the beta sheet structure. Please provide two reasons why mutating the alanine residues to arginine would be expected to disrupt the beta sheet structure.
1.Draw these phosphorylated structures as they would be connected in a polinucleotide (e.g.RNA) in the order A-B. / Show how they combine to form the polynuleotide (i.e. only the end product). Show at any one of these structures where the glycosidic bond occurs 2.Sanger sequencing revealed the sequence of an oligonucleotide to be: d-AGATGCCTGACT. Draw a diagram of the gel banding pattern post capillary electrophoresis i.e. where on the gel would the fragments feature
Polyglycine, a simple polypeptide, can form a helix with ϕ = -80°,Ψ= +150°. From the Ramachandran plot, describe thishelix with respect to handedness.
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
Please quickly
Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in
1)If we were to begin with protein that is 145 residues long, How many (ATP/GTP) would have to be used? (ATP hydrolysis from 1 pyrophosphate= 2 ATP)' 2)What is the corresponding codon of an anticodon GUA (ignoring the wobble).
Give a clear handwritten answer and explain

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