BIOCHEMISTRY II >CUSTOM<
17th Edition
ISBN: 9781337449014
Author: GARRETT
Publisher: CENGAGE C
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 6, Problem 22P
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.
Using the Active Model for concanavalin A, discuss an example in which a difference in protein primary structure leads (o a difference in protein function.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Identify the type of bond in the following disaccharides. Number your carbons to show work. Explain your answer thoroughly. Draw the number of carbons also.
Draw and explain your answer thoroughly:
a. What is the molar mass of aspirin (C9H8O4)?b. What is the mass of 0.00225mol of aspirin?c. How many moles of aspirin are present in 500mg of aspirin?
Geranylgeranyl pyrophosphate 5 is converted by general acid-base catalysis to 6, and then to the natural product 7. For clarity only limited atom numbers are shown, but the main chain carbons are numbered 1 to 16, and the off-chain methyl substituents are numbered 17-20.
A. Based on what you specified in A, use curly arrows on the drawing above to convert 5 to 6, and 6 to 7. Invoke general acids and general bases as needed, and draw in hydrogens as necessary .
B. On the structure of 7, write in the atom numbers for the carbons marked with an asterisk
Chapter 6 Solutions
BIOCHEMISTRY II >CUSTOM<
Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...
Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - 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
- α-Pinene (4) is synthesized enzymatically from nerol pyrophosphate 1. Drawn an arrow-pushing mechanism from 1 to 2 to 3 to 4; add explicit hydrogens to clarify, if needed.arrow_forwardA reverse phase column chromatography separates proteins according to their polarity. Which pentapeptide will be eluted FIRST when chromatographed at pH 7 using a reverse phase column such as a C-18 column? Peptide Sequence (from N-terminal to C-terminal) AKGED GAAVF ALLLI MCYAG GAAVF MCYAG ALLLI AKGEDarrow_forwardMelting of three DNA samples with varying lengths was monitored by increase of ultraviolet light absorbance at 260 nm. Which is the shortest DNA? A B Carrow_forward
- Select the CORRECT description of the peptide bond. The peptide bond can freely rotate around the peptide bond. The peptide bond is non-polar, hydrophobic and does not have a dipole. The peptide bond is most stable in the cis configuration. The peptide bond is rigid and planar. The peptide bond has a mix of single and double bond characters. The peptide bond is most stable in the trans configuration.arrow_forwardBelow is a fractional saturation curve for O2 binding to adult hemoglobin. Assume that curve Y represents a system at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve Z represents a system that ___________________ Curve Z: is at pH 7.4 with a higher than normal physiological level of 2,3-BPG. is at pH 7.4 with a normal physiological level of 2,3-BPG but with a decreased level of CO2. has a higher pH with a normal physiological level of 2,3-BPG. has a higher pH with a lower than physiological level of 2,3-BPG.arrow_forwardWhich is a homotropic positive effector of aspartate transcarbamoylase (ATCase)? oxygen CTP aspartate ATParrow_forward
- The reaction scheme shows the mechanism of chymotrypsin-catalyzed peptide hydrolysis. Select ALL CORRECT statements regarding the chymotrypsin mechanism. Serine is the nucleophile in the step 3. Histidine is a general base in the step 2. Carbonyl carbon is the electrophile in the step 3. Histidine is a general acid in the step 4. Carbonyl carbon is the nucleophile in the step 3. This is an example of covalent catalysis. Aspartate is the electrophile in the step 3. Histidine is the nucleophile in the step 3.arrow_forwardThe following shows a protein with mostly beta sheet secondary structures. Which force stabilizes the beta sheet secondary structure of proteins? hydrophobic interactions between nonpolar amino acid side chains within the protein. electrostatic interactions between lysine and aspartic acid residues within the protein. hydrogen bonding between hydrogen bond donors and hydrogen bond acceptors of the peptide backbone. covalent disulfide linkages between cysteine residues within the protein.arrow_forwardThe Lineweaver-Burk plot was obtained when enzyme inhibition study was done in the absence and presence of 0.50 mM inhibitor. Answer the following questions using correct units and significant figures: (a) What is the mode of inhibition, competitive, uncompetitive, mixed, or noncompetitive? Explain your answer. (b) What can you say about the finding site for the inhibitor in relation to the active site of the enzyme? Explain your answer. (c) Calculate the Km and Vmax in the absence of inhibitor. (d) Calculate the Km and Vmax in the presence of 0.50 mM inhibitor. (e) Calculate the KI of the inhibitor using the given equations for reversible inhibition. Which has a higher affinity, the substrate or the inhibitor? How can you tell?arrow_forward
- Which peptide sequence is most likely to be found in the interior portion of a water-soluble globular protein? GGDGEMG DSKSTEG GAIVLWL IVAKSLIarrow_forwardThe following shows a reaction coordinate diagram. Choose a CORRECT statement explaining the diagram. The size of C decreases in the presence of an enzyme. B indicates the activation energy of the reaction in the presence of an enzyme. C indicates the activation energy of the reaction in the presence of an enzyme. A is related to the equilibrium constant of the reaction in the absence of an enzyme.arrow_forwardSelect ALL correct statements regarding myoglobin and hemoglobin. Statements: Myoglobin has a higher affinity for oxygen than hemoglobin does. Both myoglobin and hemoglobin contain mostly alpha-helical structures. Myoglobin has one binding site for 2,3-BPG. Hemoglobin is a tetramer, each of which binds one heme group. In both myoglobin and hemoglobin, iron ions (Fe2+) bind directly to oxygen. Myoglobin is a tetrameric protein. Hemoglobin exhibits cooperative binding with oxygen. Myoglobin does not. Hydrogen ion, carbon dioxide, and 2,3-BPG are negative allosteric effectors of oxygen binding to hemoglobin. Myoglobin has a lower P50 for oxygen than hemoglobin does. Hemoglobin has a higher affinity for oxygen than myoglobin does. Both myoglobin and hemoglobin exhibit cooperative binding to oxygen.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