O Facebook - Log In or Sign UpZipGrade: Student Answer Sheet XMD9tai8v8/?tstamp=1639747989国FB2. Which of the following statements is TRUE?A. The primary structure of proteins is often depicted by ribbon diagrams where the helices are shown by corkscrews.B. Extensive denaturation changes at 2° to 4° levels, if any, may render the process irreversible.C. Keratin is a classic example of a globular protein found in human fingernails and bird feathersD. Globular proteins form part of the matrix upon which cells are arranged in animal tissues.3. If a native enzyme is composed of 124 amino acids, 8 of which are cysteine. How many disulfide bridges can be formedin the structure?А. 8В. 4.С.2D. noneA reaction system involves sucrose as the substrate and the intestinal enzyme sucrose. What will happen to the reactionrate if the pH is altered from 6.0 to 8.0 when the optimum pH is 6.2?A. Increase in reaction rateB. Decrease in reaction rateC. UnaffectedD. Inconclusive4.5. What is the type of enzyme inhibition involved if the inhibitor decreases enzyme activity by binding to a site on theother than the active site?A. Irreversible noncompetitive inhibitionB. Reversible noncompetitive inhibitionC. Irreversible competitive inhibitionD. Reversible competitive inhibitionShow all

Question 2 : The primary structure of Protein is often depicted by Ribbon diagrams where helices are…

Answered: 2. Which of the following statements is…

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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-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?
The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide 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 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 ]
DO NOT COPY OLDER ANSWERS! AND SHOW FULL WORK! I have a mixture of 4 proteins, whose sequences are shown below (note that each protein is a 100-repeat of the sequence shown). Protein A: (Gly-Ala-Lys-Val-Ile-Phe-Glu-Val-Asn-Gly) Protein B: (Ala-Ala-Lys-Arg-Ile-His-Glu-Ala-Asn-Lys) Protein C: (Glu-Val-His-Asp-Ala-Asp-Glu-Val-Asn-Asp) Protein D: (Ala-Lys-Arg-Phe-Trp-Phe-Gly-Ile-Ala-Gly) 1) Which protein/s are MOST LIKELY to precipitate out at a pH of 3.5? a) A b) B c) C d) D e) B & C f) A & D g) None of them h) Cannot be determined.
Page 1 > of 3 ZOOM B. Propose une Toie onsuinin Teguiaung Dioou giucose concentrauon. Question 2: Label the protein structure level on lines 1,2,3, and 4 and label/describe the structure to which each box corresponds. Describe the characteristics of each structural level in the boxes below. MacBook Air DII 80 888 F10 F7 FB F5 F4 F3 * & # $ 7 8 3 4 E R T Y K F M C V .. .. この * 00 B
E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o o
Suggest which part of this sequence belongs to the inner part of the protein and which to the outer shell (use the one-letter code to define amino acid. 1 letter - 1 amino acid): MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEOQWF TEDPGPDEAPRMPEAAPPGVAPTYSA
Ala-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a. pH 1.5 b. pH 8 c. pH 13
Only qno3m I think protein drawing has to show the bond interactions Onlyqno3 solve. I. Given a polypeptide below, answer the following questions: MAGGMIVIIGGMGCNSMVVVIIIGTSSCVIMEMMMIVKII Questions: 1. Enumerate all non-polar amino acids. (Provide the single letter and common name) 2. Enumerate polar amino acids include the acidic and basic types. (Provide the single letter and common name) 3. Illustrate the overall shape of the given polypeptide. Point out the specific side-chain interactions that could occur in this polypeptide by labelling the polypeptide. Defend your answer as to why your polypeptide should assume such final shape. Only accurate drawing need
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]
You will discuss the generic G protein story the rest of your career. Explain the generic story.How do the changes, when holding various G nucleotides, impact the structure of the G-protein?

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