Chemistry: Principles and Reactions
8th Edition
ISBN: 9781305079373
Author: William L. Masterton, Cecile N. Hurley
Publisher: Cengage Learning
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Textbook Question
Chapter 23, Problem 44QAP
A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein?
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Calculate the molecular weight of a small protein if 5.90 g sample of this protein is dissolved
in H₂O to make 563 mL of solution which has an osmotic pressure of 14.2 torr at 25°C.
a) 1.53 x 10³ g/mol
b) 1.37 x 104 g/mol
e) 5.81 x 105 g/mol
f) 9.74 x 106 g/mol
g) 3.37 x 102 g/mol
c) 7.23 x 10³ g/mol
d) 3.54 x 105 g/mol
The first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in the range of 0.2 to 1.0 mg/ml. For each concentration, a volume of 1.0 mL should be prepared. Describe how you will prepare these standards using a stock solution of BSA that is 2.0 mg/ml.
Answer the following questions on the basis of the free energies of formation
at 25°C shown in the table at the top of the next page:
(a) Does the peptide bond between alanine and glycine form spontaneously
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Chapter 23 Solutions
Chemistry: Principles and Reactions
Ch. 23 - Prob. 1QAPCh. 23 - Prob. 2QAPCh. 23 - Prob. 3QAPCh. 23 - Prob. 4QAPCh. 23 - Prob. 5QAPCh. 23 - Prob. 6QAPCh. 23 - Prob. 7QAPCh. 23 - Prob. 8QAPCh. 23 - Prob. 9QAPCh. 23 - Prob. 10QAP
Ch. 23 - Prob. 11QAPCh. 23 - Prob. 12QAPCh. 23 - Prob. 13QAPCh. 23 - Prob. 14QAPCh. 23 - Prob. 15QAPCh. 23 - Prob. 16QAPCh. 23 - Prob. 17QAPCh. 23 - Prob. 18QAPCh. 23 - Prob. 19QAPCh. 23 - Prob. 20QAPCh. 23 - How many chiral carbon atoms are there in ...Ch. 23 - How many chiral carbon atoms are there in sucrose?...Ch. 23 - Prob. 23QAPCh. 23 - Give the structural formulas of two different...Ch. 23 - (a) How many tripeptides can be made from glycine,...Ch. 23 - Prob. 26QAPCh. 23 - Prob. 27QAPCh. 23 - Prob. 28QAPCh. 23 - For alanine, Ka1=5.1105,Ka2=1.81010 . Calculate...Ch. 23 - Prob. 30QAPCh. 23 - On complete hydrolysis, a polypeptide gives two...Ch. 23 - Prob. 32QAPCh. 23 - Prob. 33QAPCh. 23 - Prob. 34QAPCh. 23 - Prob. 35QAPCh. 23 - Prob. 36QAPCh. 23 - Prob. 37QAPCh. 23 - Prob. 38QAPCh. 23 - Prob. 39QAPCh. 23 - Prob. 40QAPCh. 23 - Prob. 41QAPCh. 23 - Sketch the form in which leucine would exist in...Ch. 23 - How many tripeptides could one make from glycine,...Ch. 23 - A 1.00-mg sample of a pure protein yielded on...Ch. 23 - Describe what is meant by (a) the primary...Ch. 23 - Glycolysis is the process by which glucose is...Ch. 23 - Plants synthesize carbohydrates from CO2 and H2O...Ch. 23 - Prob. 48QAPCh. 23 - Prob. 49QAPCh. 23 - Prob. 50QAPCh. 23 - Prob. 51QAPCh. 23 - Aspartic acid acts as a triprotic acid with...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Explain why a protein is least soluble in an aqueous medium that has a pH equal to the isoelectric point of the protein.arrow_forward22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a substitution for leucine in the primary structure of a protein that would probably not change the character of the protein very much.arrow_forwardGive an example of amino acids that could give rise to the interactions pictured in Fig. 21-24 that maintain the tertiary structures of proteins.arrow_forward
- 22-53 Do iron and zinc ions play role in protein structure? If so, what is the role for either or both?arrow_forward22-44 How can a protein act as a buffer?arrow_forward22-85 Denaturation is usually associated with transitions from helical structures to random coils. If an imaginary process were to transform the keratin in your hair from an (-helix to a (-pleated sheet structure, would you call the process denaturation? Explain.arrow_forward
- Question 6 of 25 > Modify lysine to show the predominant form at pH 7. Modify the amino acid by adding or removing atoms or bonds and by adding charges where appropriate. Select Draw Rings More N 0 H / || III C H-O || C ▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬ H H I C *一£一£一£一£ H H I N-H Erase Q2 Qarrow_forwardAll amino acids have two ionizable functional groups: an α‑amino group (average p?a of 9.4) and an α‑carboxylic acid group (average p?a of 2.2). Aspartic acid has an ionizable side chain (R group) with a p?a of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. The protonated form of the R group of aspartic acid is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the p?a of the R group and the pH of the solution. Select all the pH values at which the charged form of the R group would predominate.arrow_forwardThe property of water solutions to conduct electric current is possible for all of the 20 standard amino acids. True or False?arrow_forward
- What are the intermolecular forces responsible for the folding of amino acid chains into proteins? Give specifics please.arrow_forward58arrow_forward12) Proteins are long chains of amino acids joined together by peptide bonds. Which structure properly depicts the peptide bond formed between two generic amino acids? 12) H. R1 H;N. N, A) R1 R2 B) R2 R2 H;N, N. R1 H R2 D) ŘIarrow_forward
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