Question 6.The solubility of globular proteins, when dissolved in water, is influenced by the factors/conditions listedbelow. Describe how these conditions would affect the solubility of the protein:a. pH of the buffer is the same as the pl of the proteinb. the pH of the solution is 12c. the solution is heated to 100°Cd. the solution contains 0.01 M NaCIc. the solution contains 70% ammonium sulphatef. the protein is dissolved in a 75% cthanol solutiong. urea is added to the solutionh. What does urea do to the protein structure?i. mercapto-ethanol is added to the solution

Globular proteins are the folded proteins that consists of hydrophilic aminoacids on the surface and…

Answered: Question 6. The solubility of globular…

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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QUESTION 2 Which peptide will most strongly attach to a carboxymethyl ion exchange column at pH 7.4? O N'-Glu-Lys-Arg-Asp-Tyr-C' O N'-Tyr-Arg-Lys-Arg-Gly-C' O N'-Gly-Glu-Gln-Asp-Asp-C' O N'-Val-Ala-Leu-lle-Arg-C' QUESTION 3 Which will be product of transcription from this double-stranded (ds) DNA sequence? 5' - atgttcaaagcctattcg - 3' 3' - tacaagtttcggataagc - 5' O YKFRIS O uacaaguuucggauaagc O auauucaaaaccuauuca Which will be product of transcription from this double-stranded (ds) DNA sequence? 5' - atgttcaaagcctattcg – 3' 3' - tacaagtttcggataagc – 5' O YKFRIS O uacaaguuucggauaagc O auguucaaagccuauucg Ο MFKAYS QUESTION 4 The structure of hemoglobin consists of a 2a and 2B heterotetramer. O quaternary O tertiary O secondary O primary
9.
1. What is the possible identity of the AA? a. Aspartic acid b. Lysine c. Alanine d. Proline 2. What is the isoelectric point of AA? 3. What is the pKa responding to the dissociation of the alpha-carboxylic group?
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
At a pH of 10.4, the protein VATSIN has a charge of а. 0 b. -.5 k. -1| d. -1.5 f -2
can you help me with this question? the list at the bottom is for part a.
Can you please explain how to solve this problem?
i need the answer quickly
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:
Only question no 12 in details
4 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pI
20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?

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