Number 4 pleas 3. Why do proteins act as buffers? Write down the appropriate chemical reactions.4. Describe the impact of protein's dipole moment on its solubility, taking albumins and globulins as examples.5. The tertiary structure of a protein involves attractions and repulsions between the side chain groups of the aminoacids of the polypeptide. What type of interactions would you expect between the R groups of the following aminoacids?• Phenylalanine and phenylalanine -• Serine and threonine-• Two cysteine residues -• Two leucine residues -

Dipoles exist when there is a separation of oppositely charges. Simple proteins are those that are…

Answered: 4. Describe the impact of protein's…

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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1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
6. Which amino acid would most likely be found on the surface of a protein molecule at physiological pH? a. Isoleucine b. Lysine c. Alanine d. Proline 7. Which of the following statements about terpenes is NOT true? a. They are a type of terpenoid. b. They all contain double bonds. c. They are all made up of 5-carbon units. d. They all contain oxygen. 8. How are the plasma membranes of mammalian and bacterial cells similar? a. They typically contain cholesterol. b. They have negatively charged lipids on their surfaces. c. They contain lipids that are involved in signal transduction. d. They are made up of many different types of phospholipids.
5 (a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
1. Explain how each primary structure of a protein affects its properties and how denaturation changes the structure. 2. Explain how each secondary structure of a protein affects its properties and how denaturation changes the structure.
6.All of the following types of interactions cooperate in stabilizing the tertiary structures of globular proteins except____. a.Disulphide bond b.Hydrogen bond c.Ionic interactions d.Peptide bond
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
1) Describe the importance of the amino acids in the structure such as the alpha helix in the secondary structure; the beta-sheet and the alpha helix in the final tertiary structure. 2) A photo of a 3D tertiary structure model of your protein using paper.
1)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?
3a) The 3° structure of a protein refers to the protein's overall, 3-dimensional shape in space. This will incorporate any 2° structure the protein has, but is predominantly the result of side-group interactions. Name the type of interaction, if any, that you would expect to see under physiological conditions (an aqueous solution at pH 7.0-7.5) between the following pairs of amino acid side groups. Serine and asparagine: Methionine and lysine: Glutamate and aspartic acid: Alanine and phenylalanine:
1. What biological molecule are required in the synthesis of protein( choose all that apply)? - phosphate ester - fatty acid (s) - alcohol - glycerol - amino acids 2. ATP is generated during A. Aldehyde reduction B. Alkene hydration C. Acetal synthesis D. Polysaccharide hydrolysis 3. What compound( biological classification) would be the result of protein complete hydrolysis in the mouth? A. Fatty acid and glycerol B. Monosaccharides C. Amino acids D. Disaccharide 4. The hydrophobic/ hydrophilic interaction are present in which protein structure level (s) (choose all that apply) ? - secondary - primary - tertiary -quaternary 5. Which protein structural level is/ are affected by the addition of an organic solvent isopropanol? A. Secondary B. Tertiary C. All are affected D. Quaternary
1. Why do proteins become polycations at extremely low pH and become polyanions at very high pH? 2. Explain why hydrogen bonding is important to protein structure.

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