3. The figure below depicts a protein folding into its final shape. If this was a cytoplasmic protein: bog go of Tertiary Structure a. The chemical properties of the amino acids in black are likely (circle): Polar or Nonpolar Primary Structure b. The chemical properties of the amino acids in white are likely (circle): Polar or Nonpolar

3. The figure below depicts a protein folding into its final shape. If this was a cytoplasmic protein: bog go of Tertiary Structure a. The chemical properties of the amino acids in black are likely (circle): Polar or Nonpolar Primary Structure b. The chemical properties of the amino acids in white are likely (circle): Polar or Nonpolar

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 8TYK: The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices...

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The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
Part A What is the highest structural level of protein structure represented in the following image? primary quaternary secondary pentanary tertiary O O
Part A What is the highest structural level of protein structure represented in the following image? tertiary primary secondary O pentanary O quaternary Submit Request Answer O O O O
1. Please come up a peptide sequence for the two proteins shown in the diagram. Multi-pass protein Single-pass protein Hydrophilic region Alpha-helical /configuration Lipid bilayer Hydrophobic region 00000 00000
4. Alpha helices, loops, and beta sheets are examples of protein secondary structure. Beta sheets can be parallel or anti-parallel. Identify all hydrogen bonds (four) in the two example sheets below. Identify which is the parallel and which is the anti-parallel. C-term Cterm H. C-term N term H. parallel anti-parallel parallel anti-parallel
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
4. Each diagram in Figure 2 below shows one level of organization of a protein. Identify each level and describe it. CA ITA (a) (b) 0 hydrogen co CH₂ bond H-0 (c) -0, 0 lonic bond C-OH H₂C H₂C CH-CH₂ amino acids -hydrophobic interactions disulfide bridge Figure 2 5. Hemoglobin is made up of four polypeptides, but also require a beme group
6. Consider the following proteins to answer the questions below: Protein Size (kDa) ε at 280 nm 10 7000 14000 3000 50000 A B C D 50 10 50 pl 4 4 8 8 Red Colored? Yes No No No a. Sketch the UV-Vis spectrum of each pure protein (A, B, C, and D) from 240- 480 nm if they were all present at 20 µM. Note: I want four clearly labeled spectra on one plot.
Give the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 B
8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3
A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.
3. Proteins are important for numerous functions in a cell and their activity/function is dependent on their structure. Each protein folds into its respective structure and ionic bonds between ions in side chains of proteins drives protein folding as shown by the oppositely charged ions in the figure below. 15 H .O H N Protein Draw a picture similar to the one shown above to show what will happen to such interactions when the pH increases. Show how this impacts protein structure. (Hint: Is the hydrogen ion concentration high or low? Note that hydrogen ions can be added or lost into molecules depending on the pH and that the NH3* is affected in this case.) Draw a picture similar to the one shown above to show what will happen to such interactions when the pH decreases. Show how this impacts protein structure. (Hint: Is the hydrogen ion concentration high or low? Note that hydrogen ions can be added or lost into molecules depending on the pH and that the COO is affected in this case.)…