3) In his haste to create the chapter 2 homework assignment, the biochemistry professor quickly drewthe structure of the polypeptide segment Ala-Lys-Thr within a larger, naturally-occurring protein chain atpH 7.4 Can you spot three mistakes the professor made?H3G'NHHH₂NHHHO||/..HCH3Mistakes:1.2.3.

Amino acids are the building blocks of proteins. They have two functional groups . Amino group and…

Answered: 3) In his haste to create the chapter 2…

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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This cartoon represents the quaternary structure of proteins and each color of the different shape represents a different subunit. 1. How many N-terminus are there in this cartoon?
TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)
Given a peptide chain that is composed of the following amino acids:(branched chain-- polar uncharged--polar positively charged -- polar negatively charged-- aromatic) 10If the component amino acids of the above peptide chain are subjected to paper chromatography, which of the amino acids will be farthest from the point of origin?
Draw the protein folding pattern when the polypeptide is immersed in water and in oil. Justify your answers by using chemical explanations. In the structure, point all possible types of intramolecular forces of attraction possible for this polypeptide in the indicated solvent system and discuss each. Discuss your answer H3N*-ala-ile-trp-arg-gly-ala-his-tyr-trp-gly-gly-tyr-arg-ile-val-thr-ile-trp-cys- met-gly-ile-asp-cys-thr-glu-cys-trp-gly-cys-phe-arg-his-pro-val-phe-CO-
-100 100 8. This is a helical wheel projection. The following amino acids of your protein were predicted to participate in an alpha helix: DRMVEHACKSI. a. Plot these amino acids in the helical wheel projection below. b. Is the alpha helix in your protein hydrophobic, amphipathic or hydrophobic? c. Would you expect this helix to be on the interior of the protein, exposed, or partially exposed?
How can a protein’s potential function be determined from a protein’s primary structure? I assumed this was not possible, I thought its function was determined from its 3-dimensional structure only. Thank you for explaining this.
The primary structure of a protein is shown below. Please answer the following questions. Leu-Arg-Ser-lle-Glu-Thr-Val-Val-Asn-Gln-Val-lle-Ser- Tyr a. Where is this section of the polypeptide most likely located [ Select ] completely embedded inside the protein partially exposed to the aqueous environment b. Is the above more likely an alpha helix or a beta-pleated sh completely exposed to the aqueous environment c. Which two amino acid residues are least likely to be in an alpha helix, but most likely to be a part of a beta turn? (Please select the amino acids in alphabetical order). [ Select ] [ Select ]
i. ii. i.v. 22. Using the figure below, answer the following questions. Identify 2 independent helices domains Identify a disordered region In the structure, box the cofactor and name it (abbreviation accepted) Using the figure, draw the structure of the cofactor bound to this protein
A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex
Please draw a single polypeptide chain structure that has the following amino acids (leucine, alanine, cystine, argenine, glutomine, and leucine) as it would appear at physiological pH. Calculate the pl of the polypeptide. I will rate!
hi, I had a question about tertiary structure. I was wondering if the properties of the R group are similar in terms of polar/non polar will that change the tertiary structure and thus function of the protein
Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientations

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