What type of IPF would you expect from the following R groups in a tertiary structure of a protein? Glutamic acid and LysineShow answer choiceslon-dipole attractionHydrogen bond attractionLondon dispersion forcesDisulfide bondSalt bridge (ion-ion attraction)Question 34What type of IPF would you expect from the following R groups in a tertiary structure of a protein? Serine and Aspartic acidShow answer choicesHydrogen bond attractionBlon-dipole attractionSalt bridge (ion-ion attraction)London dispersion forcesDE Disulfide bond0/3

The proteins are composed of twenty naturally occurring amino acids connected via peptide…

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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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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
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-
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. ΫΠΙ ΑΣΦ ха хь a b 1.73 106 ● Ĵ √x x X X |X| wwwww Submit Previous Answers Request Answer ? X.10n X orientations The problem is essentially asking about the possible combinations given that you are selecting one of three items a set number of times. It may help to think of a concrete example. If you roll a standard six-sided die, the first roll has six possible combinations. The second roll also has six possible combinations; however, when paired with the first there are 6 x 6 possible sets of numbers. Provided the order of the numbers matters, when rolling a third time there are 6 x 6 × 6 possible sets of numbers. This pattern is 6" where r is the number of rolls. For this problem, there are three possible selections. There are 120…
Given the following peptide, answer following questions 1-5: CO CH2 O || CH2 O H3N-CH-C-NH- CH-c-OCH3 | 1. Is this a dipeptide or tripeptide? 2. How many amino acid components/residues are there? 3. Name these amino acids. 4. What kind of bond links these amino acids? 5. The above structure represents the major ingredient in some commercial product(s). Identify the name of this major ingredient or the commercial product(s). Given that the hemagglutininin protein in influenza virus contains a remarkably long a-helix with 53 residues, answer questions 6-7. 6. How long is this a-helix (in nm)? Show all calculations. 7. How many turns does this helix have? Show all calculations.
Given below is a sequence of a polypeptide: AVLLRKIFWFDLAG The pKas of different groups/side chains are shown in the table below: Group/side chain pka C-terminus 3.5 Asp 3.9 Glu 4.1 His 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 N-terminus 9.0 What is the total charge of this molecule at pH 11? [ Select ] What is the total charge of this molecule at pH 13? [ Select ] What is the isolectric point for this molecule? (Select]
Given below is a sequence of a polypeptide: AVLLRKIFWEDLAG The pKas of different groups/side chains are shown in the table below: Group/side chain pka C-terminus 3.5 Asp 3.9 Glu 4.1 His 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 N-terminus 9.0 What is the total charge of this molecule below pH 3.5? [ Select ] What is the total charge of this molecule at pH 5? [Select ]
A protein with a known mass of 240 kDa is treated with -mercaptoethanol, a sulfhydryl reducing agent. When the resultant peptide mixture was analyzed by SDS PAGE, one protein band of 60 kDa was present. How many disulfide bonds were present in the original structure of the protein? Group of answer choices -4 -2 -1 -3
697149&page%3D2 ning System (Academic) 49 When we refer to the backbone of a polypeptide, we are referring to the attachment between: Select one: out of O a. The amino, carboxyl group and the oa-carbon O b. The peptide bond between two amino groups question O c. The amino acids making the polypeptide O d. The amino and carboxyl groups only O e. The R groups of the amino acids Which of the following molecules is a polymer made from large number of building blocks called monomers linked together by covalent bonds? 50 out of Select one: O a. Glucocorticoids, a steroid hormone question O b. Waxes (such as beeswax) O c. Glycogen, that stored in liver cells O d. Cooking oils O e. Stearic acid (saturated fatty acids)
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?
The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds
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?)
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…

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What type of IPF would you expect from the following R groups in a tertiary structure of a protein? Glutamic acid and Lysine Show answer choices lon-dipole attraction Hydrogen bond attraction London dispersion forces Disulfide bond Salt bridge (ion-ion attraction)