Organic Chemistry
8th Edition
ISBN: 9781305580350
Author: William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher: Cengage Learning
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Chapter 27, Problem 27.57P
Interpretation Introduction
Interpretation:
Three common denaturing agents are SDS (Sodium dodecyl sulphate), Urea and Heat. In proteins what kinds of non-covalent interactions each reagent disrupt has to be given.
Concept Introduction:
Denaturation causes the physical change in the protein molecule. It gives the observable changes like the loss of biological activity. The denaturation occurs by the changes in the secondary, tertiary and quaternary structures by the disruption of non-covalent interactions of hydrogen bonding and hydrophobic interactions.
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Check out a sample textbook solutionChapter 27 Solutions
Organic Chemistry
Ch. 27.1 - Of the 20 protein-derived amino acids shown in...Ch. 27.2 - Prob. 27.2PCh. 27.2 - Prob. 27.3PCh. 27.3 - Draw a structural formula for Lys-Phe-Ala. Label...Ch. 27.4 - Which of these tripeptides are hydrolyzed by...Ch. 27.4 - Deduce the amino acid sequence of an undecapeptide...Ch. 27.6 - Prob. 27.7PCh. 27 - What amino acid does each abbreviation stand for?...Ch. 27 - The configuration of the chiral center in -amino...Ch. 27 - Assign an R or S configuration to the chiral...
Ch. 27 - Prob. 27.11PCh. 27 - Prob. 27.12PCh. 27 - Draw zwitterion forms of these amino acids. (a)...Ch. 27 - Prob. 27.14PCh. 27 - Why is Arg often referred to as a basic amino...Ch. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Both norepinephrine and epinephrine are...Ch. 27 - Prob. 27.22PCh. 27 - Draw a structural formula for the form of each...Ch. 27 - Prob. 27.24PCh. 27 - Write the zwitterion form of alanine and show its...Ch. 27 - Prob. 27.26PCh. 27 - Write the form of aspartic acid most prevalent at...Ch. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - For lysine and arginine, the isoelectric point,...Ch. 27 - Prob. 27.31PCh. 27 - Account for the fact that the isoelectric point of...Ch. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - At pH 7.4, the pH of blood plasma, do the majority...Ch. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - A chemically modified guanidino group is present...Ch. 27 - Draw a structural formula for the product formed...Ch. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - A decapeptide has the following amino acid...Ch. 27 - Following is the primary structure of glucagon, a...Ch. 27 - Prob. 27.45PCh. 27 - Draw a structural formula of these tripeptides....Ch. 27 - Estimate the pI of each tripeptide in Problem...Ch. 27 - Glutathione (G-SH), one of the most common...Ch. 27 - Following are a structural formula and a...Ch. 27 - Prob. 27.50PCh. 27 - Prob. 27.51PCh. 27 - Prob. 27.52PCh. 27 - Prob. 27.53PCh. 27 - Prob. 27.54PCh. 27 - Distinguish between intermolecular and...Ch. 27 - Prob. 27.56PCh. 27 - Prob. 27.57P
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- 22-49 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_forwardDo the amino acid sequences: valine-asparagine and asparagine-valine represent the same compound? Explain.arrow_forwardFor the tripeptide SerArgIle which amino acid residues a. are hydrophilic b. are hydrophobic c. possess polar neutral R groups d. participate in two amide linkagesarrow_forward
- Is the primary, secondary, or tertiary structure of a protein changed by denaturation?arrow_forward(a) How many tripeptides can be made from glycine, alanine, and leucine, using each amino acid only once per tripeptide? (b) Write the structural formulas of these tripeptides and name them in the shorthand abbreviation used for showing amino acid sequences.arrow_forward22-53 Do iron and zinc ions play role in protein structure? If so, what is the role for either or both?arrow_forward
- 22-85 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. How many unique amino acid sequences are possible for a tripeptide containing only the amino acids gly, ala, and cys, with each amino acid occurring only once in each molecule?arrow_forwardIn a pleated sheet secondary structure for a protein a. describe the general shape of the protein backbone b. describe the general locations for the amino acid R groupsarrow_forward
- Fill in the blanks in the following statements: aThe order of the amino acids in a protein is the ______ structure of that protein. The _______ of the backbone chain of a protein is the secondary structure of that protein. The tertiary structure of a protein describes the ______ of the secondary structure. b Hydrogen bonding between the oxygen atoms of carbonyl groups and the hydrogen atoms of amide groups in the same protein chain gives the secondary structure, called the ______. c Hydrogen bonding between the oxygen atoms of carbonyl groups and the hydrogen atoms of amide groups in the adjacent protein chain gives the secondary structure, called the ______.arrow_forwardWhat functional groups are found in all amino acids? How many different amino acids are found in naturally occurring proteins?arrow_forward
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