Anatomy & Physiology: The Unity of Form and Function
9th Edition
ISBN: 9781260791563
Author: Kenneth S. Saladin
Publisher: Mcgraw-hill Higher Education (us)
expand_more
expand_more
format_list_bulleted
Question
Chapter 2.4, Problem 20BYGO
Summary Introduction
To determine: The protein structure that changes itself when heated.
Introduction: Proteins are large and complex
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Which is more likely to be changed by heating a protein, its primary structure or its tertiary structure? Explain.
Using condensed structures, supply an outline of the mechanism for the formation of Gly-Gly in the
human body. (Hint: It is not a simple condensation reaction).
Explain how a protein is denatured by the following: (a) Heat(b) Strong acids (c) Organic solvents
Chapter 2 Solutions
Anatomy & Physiology: The Unity of Form and Function
Ch. 2.1 - Prob. 1BYGOCh. 2.1 - Prob. 2BYGOCh. 2.1 - Prob. 3BYGOCh. 2.1 - Prob. 4BYGOCh. 2.1 - Prob. 5BYGOCh. 2.1 - The definition of chemical element; the six most...Ch. 2.1 - The structure of an atom and the special...Ch. 2.1 - Prob. 3AYLOCh. 2.1 - Prob. 4AYLOCh. 2.1 - Prob. 5AYLO
Ch. 2.1 - Prob. 6AYLOCh. 2.1 - Prob. 7AYLOCh. 2.1 - Prob. 8AYLOCh. 2.1 - Hew isomers resemble and differ from each otherCh. 2.1 - Prob. 10AYLOCh. 2.1 - Prob. 11AYLOCh. 2.2 - Prob. 6BYGOCh. 2.2 - Prob. 7BYGOCh. 2.2 - Prob. 8BYGOCh. 2.2 - Prob. 9BYGOCh. 2.2 - Prob. 10BYGOCh. 2.2 - Prob. 11BYGOCh. 2.2 - How the biologically important properties of water...Ch. 2.2 - Prob. 2AYLOCh. 2.2 - The differences between solutions, colloids, and...Ch. 2.2 - Prob. 4AYLOCh. 2.2 - The action and physiological function of buffersCh. 2.2 - Prob. 6AYLOCh. 2.3 - Prob. 12BYGOCh. 2.3 - Prob. 13BYGOCh. 2.3 - Prob. 14BYGOCh. 2.3 - Prob. 15BYGOCh. 2.3 - The definition of energy, and the two basic forma...Ch. 2.3 - Prob. 2AYLOCh. 2.3 - Prob. 3AYLOCh. 2.3 - Prob. 4AYLOCh. 2.3 - Prob. 5AYLOCh. 2.3 - Prob. 6AYLOCh. 2.4 - Prob. 16BYGOCh. 2.4 - Prob. 17BYGOCh. 2.4 - Prob. 18BYGOCh. 2.4 - Prob. 19BYGOCh. 2.4 - Prob. 20BYGOCh. 2.4 - Prob. 21BYGOCh. 2.4 - Prob. 22BYGOCh. 2.4 - Prob. 23BYGOCh. 2.4 - Prob. 24BYGOCh. 2.4 - The criterion for considering a compound to be...Ch. 2.4 - Prob. 2AYLOCh. 2.4 - The structures of hydroxyl, methyl, carboxyl,...Ch. 2.4 - The difference between monomer and polymera; how...Ch. 2.4 - The defining characteristics of carbohydrates end...Ch. 2.4 - Prob. 6AYLOCh. 2.4 - Prob. 7AYLOCh. 2.4 - Prob. 8AYLOCh. 2.4 - Prob. 9AYLOCh. 2.4 - Prob. 10AYLOCh. 2.4 - Prob. 11AYLOCh. 2.4 - Differences between a dipeptide, oligopeptide,...Ch. 2.4 - Prob. 13AYLOCh. 2.4 - Prob. 14AYLOCh. 2.4 - What defines a conjugated protein; the general...Ch. 2.4 - Prob. 16AYLOCh. 2.4 - How enzymes differ from ether proteins, and the...Ch. 2.4 - Prob. 18AYLOCh. 2.4 - Prob. 19AYLOCh. 2.4 - The term for a chain of linked enzymatic...Ch. 2.4 - The basic structural components of adenosine...Ch. 2.4 - Prob. 22AYLOCh. 2.4 - Prob. 23AYLOCh. 2.4 - Prob. 24AYLOCh. 2 - A substance that ____ is considered to be a...Ch. 2 - Prob. 2TYRCh. 2 - Prob. 3TYRCh. 2 - Prob. 4TYRCh. 2 - Prob. 5TYRCh. 2 - Prob. 6TYRCh. 2 - Prob. 7TYRCh. 2 - The arrangement of a polypeptide into a fibrous or...Ch. 2 - Prob. 9TYRCh. 2 - Prob. 10TYRCh. 2 - Prob. 11TYRCh. 2 - Dietary antioxidants are important because they...Ch. 2 - Prob. 13TYRCh. 2 - Prob. 14TYRCh. 2 - A chemical reaction that joins two organic...Ch. 2 - Prob. 16TYRCh. 2 - Prob. 17TYRCh. 2 - Prob. 18TYRCh. 2 - Prob. 19TYRCh. 2 - Prob. 20TYRCh. 2 - Prob. 1BYMVCh. 2 - Prob. 2BYMVCh. 2 - Prob. 3BYMVCh. 2 - Prob. 4BYMVCh. 2 - Prob. 5BYMVCh. 2 - Prob. 6BYMVCh. 2 - Prob. 7BYMVCh. 2 - Prob. 8BYMVCh. 2 - Prob. 9BYMVCh. 2 - Prob. 10BYMVCh. 2 - Prob. 1WWTSCh. 2 - Prob. 2WWTSCh. 2 - Prob. 3WWTSCh. 2 - Prob. 4WWTSCh. 2 - Prob. 5WWTSCh. 2 - Prob. 6WWTSCh. 2 - Prob. 7WWTSCh. 2 - The higher the temperature is, the faster an...Ch. 2 - Prob. 9WWTSCh. 2 - Prob. 10WWTSCh. 2 - Suppose a pregnant women with serve morning...Ch. 2 - Prob. 2TYCCh. 2 - Prob. 3TYCCh. 2 - How would the bodys metabolic rate be affected if...Ch. 2 - Prob. 5TYC
Knowledge Booster
Similar questions
- Explain briefly why the ionizable properties of amino acids are so crucial in the structure and function of proteins.arrow_forwardb) The likelihood of both triglycerides and phospholipids to behave as liquids at a given temperature is affected by their degree of saturation. Explain what saturation is and provide a biochemical explanation for why it affects the likelihood of a lipid to behave as a liquid at a given temperature. 5) a) Proteins have multiple "levels" of structural complexity. Match the type of chemical bond on the left with the level of protein structure that they are specifically involved in maintaining on the right. (Note that more than one letter may apply to each structural level and that each letter may be used more than once or not at all). a. disulphide bonds Tertiary structure b. hydrogen bonds Primary structure c. ionic bonds Quaternary structure d. peptide bonds Secondary structurearrow_forwardA) Refer to the figure below, Identify and explain the two types of reactions, and describe what are the importance of these reactions to our bodies. Reaction 1 H Monomer Reaction 2 H H OH + H H H₂O H H₂O OH + H H OH OH + H H₂O H₂O OH OH + H OH OH OH OH B) What are the main chemical interactions that determine and maintain the quaternary structure of proteins. Also, what are the conditions that can alter these interactions? [arrow_forward
- What is amphoterism? Show using chemical equations the amphoteric property of protein.arrow_forwardDescribe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.arrow_forwardThe pka of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH 6.4? 15.3% 28.5% 45.3% O 66.6%arrow_forward
- a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?arrow_forwardDisulfide bonds help to stabilize the three-dimensional structure of proteins. What amino acids are involved in the formation of disulfide bonds? Does the formation of a disulfide bond increase or decrease entropy (ΔS)?arrow_forwardDenatured protein is in a low energy state. What sort of explanation can you use to rationalize that statement? Hint: consider Gibbs free energy.arrow_forward
- Most protein dissolve in neutral salt solution, is that true? Provide reasoningarrow_forwardWhy is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.arrow_forwardExplain what is meant by "The Central Dogma"? In your explanation, describe the structure and function of the macromolecules that are important in this process. Describe at least two deviations to the Central Dogma.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning