Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 4, Problem 14P
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
A Rule of Thumb for Amino Acid Content in Proteins The simple average molecular weight of the 20 common amino adds is 138, but most biochemists use 110 when estimating the number of amino acids in a protein of known molecular weight. Why do you Suppose this is?
(Hint: There are two contributing factors to the answer. One of them will be apparent from a brief consideration of the amino acid compositions of common proteins. See, for example, Figure 5.16 of this text.)
Expert Solution & Answer
Trending nowThis is a popular solution!
Chapter 4 Solutions
Biochemistry
Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...
Ch. 4 - Prob. 11PCh. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...Ch. 4 - Answers to all problems are at the end of this...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. (Research Problem) The Nature and Roles of Linear Motifs in Proteins In addition to domains and modules, there are other significant sequence patterns in proteins—known as linear motifs—that are associated with a particular function. Consult the biochemical literature to answer the following questions: 1. What are linear motifs? 2. How are they different from domains?. 3. What are their functions? 4. How can they be characterized? 5. There are several papers that are good starting points for this problem. Neduva, V., and Russell, R., 2005. Linear motifs: evolutionary interaction switches. FEBS Letters 579:3342-3345. Gibson, T., 2009. Cell regulation: determined to signal discrete cooperation. Trends in Biochemical Sciences 34:471-482. Diella, K. Haslam, N., Chica., C. et aL, 2009. Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Frontiers of Bioscience 13:6580-6603.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. To fully appreciate the elements of secondary structure in proteins, it is useful to have a practical sense of their structures. On a piece of paper, draw a simple but large zigzag pattern to represent a -strand. Then fill in the structure, drawing the locations of the moms of the chain on this zigzag pattern. Then draw a simple, large coil on a piece of paper to represent an -helix. Then fill in the structure, drawing the backbone atoms in the correction locations along the coil and indicating the locations of the R groups in your drawing.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Draw the Titration Curve for a Weak Acid and Determine its pKa from the Titration Curve When a 0.1 M solution of a weak acid was titrated with base, the following results were obtained: Plot the results of this titration and determine the pK a of the weak acid from your graph.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. The Role of Proline Residues in -Turns Pro is the amino acid least commonly found in «-helices but most commonly found in -turns. Discuss the reasons for this behavior.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculating pH in Amino Acid Solutions II (Integrates with Chapter 2.) Calculate the pH at which the -amino group of lysine is 20% dissociated.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems book. Understanding the Role of Gly Residues In Protein Secondary and Tertiary Structure It is often observed that Gly residues are conserved in proteins to a greater degree than other amino acids. From what you have learned in this chapter, suggest a reason for this observation.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Assessing the pH Dependence of Poly-L-Glutamate Structure Poly-L glutamate adopts an tr-helical structure at low pH but becomes a random coil above pH 5. Explain this behavior.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Writing Dissociation Equations for Amino Acids Write equations fur the ionic dissociations of alanine, glutamate, histidine, lysine, and phenylalanine.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Assessing the Range of and Angles in Proteins Choose any three regions in the Ramachandran plot and discuss the likelihood of observing that combination of and in a peptide or protein. Defend your answer using suitable molecular models of a peptide.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Use examples from the ActiveModel for Human GaleLtin-1 to describe the hydrophobic effect.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Determining the Systematic Name for a Trisaccharide Give the systematic name for it stachyose.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Consider a protein that can exist in two forms: folded and unfolded. Calculate the free energy difference at 298 k. between a state in which SU% of the protein is folded and a state in which 80%of the protein is unfolded.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Chapter 7 - Human Movement Science; Author: Dr. Jeff Williams;https://www.youtube.com/watch?v=LlqElkn4PA4;License: Standard youtube license