Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 5, Problem 55TQ
Summary Introduction
To review:
The way in which protein molecules incorporate large amounts of immobilized water and make it a part of their structure.
Introduction:
Water playsan important role in governing the structure and stability of proteins. Water molecules participate in hydrogen bonding and electrostatic interactions with the side chains of amino acids present on the surface of the protein. In the structure of a protein, there are hydrophobic side chains that are excluded from the water. These increase the entropy of water molecules.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Question 4. Imagine the main chain of a protein bends
back on itself so that two amino acid residues R1 and R2
come close to each other.
In the table below are four possibilities for what R1 and
R2 might be. In each case, decide whether a specific
interaction could form between the residues. If a specific
interaction could form, give the name of the interaction.
R₁
cysteine
tyrosine
threonine
arginine
R₂
cysteine
phenylalanine
glutamine
aspartate
specific
interaction?
OO
yes
O yes
O no
no
OO
O yes
no
yes
no
name of specific
interaction
0
П
0
0
Question 25
Calculate the net charges of the following peptides at pH 7.4. Indicate which amino acids bear chuarged side chans
a) NH2-Asp-Leu-Phe-Ala-Lys-Pro-Glu-Gly-COOH
b) NH2-GIn-Glu-Lys-Tyr-Trp-Arg-Ala-Leu-COOH
DELL
Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
Chapter 5 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 5 - Prob. 1QCh. 5 - Prob. 2QCh. 5 - Prob. 3QCh. 5 - Prob. 4QCh. 5 - Prob. 5QCh. 5 - Prob. 6QCh. 5 - Prob. 7QCh. 5 - Prob. 8QCh. 5 - Prob. 9QCh. 5 - Prob. 10Q
Ch. 5 - Prob. 11QCh. 5 - Prob. 12QCh. 5 - Prob. 1RQCh. 5 - Prob. 2RQCh. 5 - Prob. 3RQCh. 5 - Prob. 4RQCh. 5 - Prob. 5RQCh. 5 - Prob. 6RQCh. 5 - Prob. 7RQCh. 5 - Prob. 8RQCh. 5 - Prob. 9RQCh. 5 - Prob. 10RQCh. 5 - Prob. 11RQCh. 5 - Prob. 12RQCh. 5 - Prob. 13RQCh. 5 - Prob. 14RQCh. 5 - Prob. 15RQCh. 5 - Prob. 16RQCh. 5 - Prob. 17RQCh. 5 - Prob. 18RQCh. 5 - Prob. 19RQCh. 5 - Prob. 20RQCh. 5 - Prob. 21RQCh. 5 - Prob. 22RQCh. 5 - Prob. 23RQCh. 5 - Prob. 24RQCh. 5 - Prob. 25RQCh. 5 - Prob. 26RQCh. 5 - Prob. 27RQCh. 5 - Prob. 28RQCh. 5 - Prob. 29RQCh. 5 - Prob. 30RQCh. 5 - Prob. 31RQCh. 5 - Prob. 32FBCh. 5 - Prob. 33FBCh. 5 - Prob. 34FBCh. 5 - Prob. 35FBCh. 5 - Prob. 36FBCh. 5 - Prob. 37FBCh. 5 - Prob. 38FBCh. 5 - Prob. 39FBCh. 5 - Prob. 40FBCh. 5 - Prob. 41FBCh. 5 - Prob. 42SACh. 5 - Prob. 43SACh. 5 - Prob. 44SACh. 5 - Prob. 45SACh. 5 - Prob. 46SACh. 5 - Prob. 47TQCh. 5 - Prob. 48TQCh. 5 - Prob. 49TQCh. 5 - Prob. 50TQCh. 5 - Prob. 51TQCh. 5 - Prob. 52TQCh. 5 - Prob. 53TQCh. 5 - Prob. 54TQCh. 5 - Prob. 55TQCh. 5 - Prob. 56TQCh. 5 - Prob. 57TQCh. 5 - Prob. 58TQCh. 5 - Prob. 59TQCh. 5 - Prob. 60TQCh. 5 - Prob. 61TQCh. 5 - Prob. 62TQCh. 5 - Prob. 63TQCh. 5 - Prob. 64TQCh. 5 - Prob. 65TQCh. 5 - Prob. 66TQCh. 5 - Prob. 67TQCh. 5 - Prob. 68TQCh. 5 - Prob. 69TQCh. 5 - Prob. 70TQ
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
- When a purine or a pyrimidine is linked through a β-N-glycosidic link to C-1 of a pentose, the molecule is called a _____________ .arrow_forwardAdenine and guanine are examples of the_________________________ class of nitrogenous bases.arrow_forwardThe detergent sodium dodecyl sulfate (SDS) denatures proteins. Suggest how SDS destroys protein structure.arrow_forward
- When a purine or pyrimidine is linked through a b-Nglycosidic link to C-1 of a pentose, the molecule is calleda _________________________.arrow_forwardQuestion 28 : In a SDS-PAGE analysis (Indicate the right answer) : A- The proteins are denatured and positively charged by the addition of SDS. B- Large proteins run faster than small proteins. C- If the pHi of a protein corresponds to the pH of the running buffer the protein becomes positively charged (+) and cannot migrate anymore into the gel. D- For reducing disulfide bridges one needs to add a reducing agent such as 2-mercaptoethanol or DTT. E- All is wrong.arrow_forwardA posttranslational modification that directs a polypeptide toa specific site is called a _____________________modification.arrow_forward
- The _____________ is an explanation for why there are fewer tRNAs than expected in living cells.arrow_forwardQuestion 18 There is energy requirement for every amino acid added in a growing polypeptide chain. A) True B) Falsearrow_forwardAll sugar residues are in their D-isomeric forms. As drawn, there are ________ chiral carbons in this trisaccharide.arrow_forward
- There are several sugars along with fructose and glucose that are isomeric, name them.arrow_forwardCan you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.arrow_forwardSuggest a reason (or reasons) why amino acids polymerize to form proteins that have comparatively few covalent crosslinks in the polypeptide chain.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON