Theoretical Questions1. Draw the general structure of the zwitterion form of an amino acid using the letter R for the sidechain group. What is the term given for the pH range at which an amino acid exists in thezwitterion form?2. What functional group results when amino acids are linked together?3. Give the four different classifications for amino acids. Which ones have side chains that couldhave a charge?4. Define Denaturation. Changes in which levels of protein structure could cause denaturationcould occur?

Below is the general structure of an amino acid's zwitterion form using the letter R as its side…

Answered: Theoretical Questions 1. Draw the…

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Instruct 1. What is a peptide bond? Pre-Lab Study Questions 2. How does the primary structure of proteins differ from the secondary structure? 3. Write the 1- and 3-letter abbreviations of the 6 tripeptides possible from Ala, Pro, Ser. 4. Draw the condensed structural formula of the dipeptide Phe-Val (FV).
Part C and D
1a. Describe the formation of a bond between two amino acids that craves a peptide. 1B. The image below is a dipeptide. How can you always identified the peptide bond between amino acids?
Researchers discover a new amino acid. Its R-group exclusively has hydrogen and carbon atoms. What behavior will this amino acid show? O Relative to the amino acids found in organisms, its interactions with water will be very high. It is hydrophilic. Relative to the amino acids found in organisms, its interactions with water will be intermediate. It is hydrophobic.
please help and explain clearly for me
Explain why casein precipitates when vinegar is added. Why was milk or raw egg once used as an antidote in cases of heavy metal poisoning? Based on your isolated yield of casein, how many grams of the protein are in one 200 g glass of milk? Which of the solutions contained amide bonds? Which test tells you this? Which of the solutions contained compounds with primary amino groups? Which test tells you this? Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions?
6. Is this amino acid L- or D-, and how can you tell? Н -ŅH3 CH3 a. D-, because all amino acids are D. b. D-, because the amine is on the right. c. D-, because the amine is on the left. d. L-, because the amine is on the left.
Draw a diagram of 2 amino acids and illustrate where the bond occurs. a. Encircle where the bond occurs b. What kind of reaction is occurring?
H N. NH3 'N' NH3 NH Part A What are the amino acids in kyotorphin? Spell out the full names of the compounds. Enter your answers separated by a comma. Submit Request Answer Part B How would you name the dipeptide in kyotorphin? Spell out the full name of the compound.
Select all that apply Select all the statements that correctly describe protein formation. Multiple select question. Proteins are formed between amino acid monomers. Proteins are biological addition polymers. When the carboxy group reacts with the amino group to form the protein, a carbon dioxide molecule is eliminated. Proteins are formed when the amino group of one monomer reacts with a carboxy group of another.
Amino Acids Properties: Match the following specific "R" groups of amino acids to the descriptions. nonpolar, polar neutral, polar acidic, polar basic Definition Word fill in blank -СН2-CH2-СH2-Снз -CH2-CO0- fill in blank fill in blank benzene -CH2-CH2-CH2-Cн2- fill in blank NH3+ -CH2-SH fill in blank fill in blank -CH2-OH please explain each than give answer
Which interaction(s) is/are involved in the primary structure of a protein (choose all that apply)? a. hydrogen bonding b. salt bridge c. hydrophobic effects d. covalent peptide bond

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