4. What is the molecular basis for the observation that the overall charge on a protein becomesincreasingly positive as pH drops and more negative as pH increases?

Proteins perform a wide variety of activities, which is enabled by the diversity of amino acid…

Answered: 4. What is the molecular basis for the…

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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5. Classify each of the following amino acids as polar or nonpolar and hydrophilic and hydrophobic. NH2 CH2 CH2 H2N-C-COOH H2N-C-COOH H. a. b. Polar or nonpolar: Hydrophilic or Hydrophobic:
32) You are working with an molecule with a pl of 6.00 and the pKa's of the ionizable groups on the molecule are 1.3, 4.1 and 7.9. You would like this amino acid to have a net negative charge. Which of the following pH values would result in a net negative charge? A) 1.3 B) 4.1 C) 4.43 D) 6.0 E) 7.9
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
4. Explain and draw a representative picture of the four levels of protein structure. How are they defined and what bonds keep them together? ? What effect does the a
4. A protein solution is prepared by dissolving 350 µg of protein in 200 µL of water. A 150 μL sample of this solution is diluted to a total volume of 4.5 mL. How many mg of protein will be in a 2 mL sample of the diluted protein solution? Space to show your workings:
5. Bread contains mixture of polypeptides known as gluten. This polypeptide has two types which are gliadins and glutenins. If both polypeptides have presence of short a-helix sections because of high proline content, what level of protein structure is being depicted? 5a. If intermolecular bonds form between glutenin and gliadin, what level of protein structure is being depicted? 5b. During analysis, hydrophobic amino acids (i.e., glutamine and proline) were not found on gluten protein surfaces. In this case, what level of protein structure is being shown?
4.) If a mutation in an organisms DNA causes the resulting protein to possess an alanine residue to be in the 13th position instead of a glycine, what level(s) of the resulting protein's structure would likely be affected? Why? Why would the other(s) not be affected? 14:
7. You want to separate these four proteins in a mixture: Isoelectric point Mol. Weight (kDa) Protein A 4.1 80 Protein B 9.0 81 Protein C 8.8 37 Protein D 3.9 172 Which of the following would be the best order in which to run chromatography columns? A) Anion-exchange at pH 3, then size exclusion B) Cation-exchange at pH 3, then size exclusion C) Cation-exchange at pH 3, then anion-exchange at pH 3 D) Anion-exchange at pH 3, then cation-exchange at pH 3 E) Size exclusion, then cation-exchange at pH 3 F) Size exclusion, then anion-exchange at pH 3
32. Would you expect to find hydrophobic amino acids on the external surface or internally in proteins? Why?
9. Identify the N-terminal and C-terminal amino acid in each peptide. H,N-CH-C-Ņ–CH-C-o- CH2 H CH3 ČH(CH3)2 HÑ-CH-C-Ņ-CH-C-N–CH–C-O- CH2 H ČH3 H ČH,CH,CONH, a.
3. A biochemist purified a protein from the bloodstream and determined its molecular weight under several conditions. In 8 M urea, which denatures the polypeptide chain, the molecular weight of the protein was 150,000 Da. She found that under reducing conditions the molecular weight of the protein was 75,000 Da, while under oxidizing conditions the molecular weight of the protein was 150,000 Da. Explain these results.
3. One of the 20 standard amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? What is its three-letter abbreviation and one-letter code? Write the chemical structure of this amino acid at physiological pH.

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4. What is the molecular basis for the observation that the overall charge on a protein becomes increasingly positive as pH drops and more negative as pH increases?