What to submit: Draw in the hydrogen bonds for parallel and antiparallel sheets and replacethe current image with new ones. Underline the correct sheet type. Submit as an image orPDF.Label the amino acids in the following peptide using their three-letter and one letter codeH₂NOHThree Letter Code -One Letter Code -ZIIZZINH₂Draw out the following peptide (CHARLIE) from N to C terminus. Draw by hand andupload as a file attachment. What is the net charge of your peptide?net charge:+

The proteins are a major class of biological macromolecules that are composed of amino acids…

Answered: What to submit: Draw in the hydrogen…

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

Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
Given below are sequences of amino acids present in an oligo-peptide chain. Count the overall charge of each assigned peptide and write it in your answer. Along with it also mention that toward which electrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-Val
Examine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.
complete the sentence In the Sanger method, the nitrogen from the tripeptide (give the name of the tri-peptide using the one-letter-codes of the 3 amino acids forming it, no spaces or punctuation between letters. eg. ABC) (. ) shown above acts as a ( )
Which of the numbered bonds in this polypeptide fragment are peptide bond(s)? (Select all that apply!)
Assign IUPAC names to each of the following small peptides.Gly-Ala-Leu Gly-Tyr-Ser-Ser
draw a “trans” and a “cis” peptide bond of alanine and threonine with the peptide bond lying in the plane of the paper. Draw a second view of each peptide bonds now looking down/along the peptide bond (i.e. one atom of the peptide bond will be in front and will obscure the second one behind it). Using a circular arrow, demonstrate how the torsion angle can be directly “read” from the picture. You can do this with an accuracy of ~10°. Provide an explanatory caption.
Please calculate and plot the charge on a peptide with the sequence of NEYK over the pH range from 1 to 13. Please use the pKa values from the table. You may calculate the charge at 1 pH unit intervals.
The following is an assignment question I wrote and then submitted to the AI chatbot – ChatGPT: a poly glutamic acid peptide can form an alpha helix at pH 2.4 but not at pH 7.5, why? Here is the response the AI gave me: “Poly glutamic acid is a peptide composed of multiple units of the amino acid glutamic acid. At low pH, such as pH 2.4, the glutamic acid residues in the peptide are protonated and carry a positive charge. At high pH, such as pH 7.5, the glutamic acid residues are deprotonated and carry a negative charge. The formation of an alpha helix in a peptide is primarily driven by hydrogen bonding between the amide groups of the peptide backbone. At low pH, the positive charges on the glutamic acid residues can interact with the negative charges on the backbone amide groups, stabilizing the helix conformation. However, at high pH, the negative charges on the glutamic acid residues repel the negative charges on the backbone amide groups, destabilizing the alpha helix…
This diagram shows the allowed rotations about the backbone of a peptide: Sigmoidal Curve Homology Matrix Ramachandran Plot BLOSUM
Draw out this peptide using condensed or line-bond structures: His-Thy-Phe-Cys-Glu examine your drawing of peptide for each amino acid, indicate what type(s) of interactions it can contribute to protein tertiary structure
Label: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.

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