![Biochemistry](https://www.bartleby.com/isbn_cover_images/9781464126109/9781464126109_largeCoverImage.gif)
Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 2, Problem 21P
Interpretation Introduction
Interpretation:
The groups in a protein that can form hydrogen bonds or electrostatic bonds with an arginine side chain at pH 7, needs to be identified.
Concept introduction:
Amino acids are the building blocks of proteins and Protein plays a vital role in almost all biological processes. A huge proportion of our cells, tissue and muscles are made up of amino acids, means they carry out several significant bodily functions, like, providing cells their structure.
Expert Solution & Answer
![Check Mark](/static/check-mark.png)
Want to see the full answer?
Check out a sample textbook solution![Blurred answer](/static/blurred-answer.jpg)
Students have asked these similar questions
Need help.
Which one of the following statements is FALSE?
Group of answer choices
A.Beta-pleated sheets are part of the secondary structure of proteins
B.The nitrogenous bases of DNA are located on the inside because they are hydrophobic in character
C.The peptide bond is formed by dehydration synthesis
D.Alpha helices are stabilized by attraction between the amino acid R groups
E.The peptide bond is rigid and planar and has partial double bond character
. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids.
Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr
– Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala
– Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.
Beta folding. Parallel and antiparallel beta folding sheets (be able to draw). Beta loops. Examples of proteins formed mainly by this structure.
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34P
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
- 7 Protein structure.Circle one of the three amino acid sequences that is most likely to form a stable a-helix? RASKTARQ DASKTAEQ KPGKPAGQ In one sentence (that can be accompanied by a small picture) explain why?arrow_forwardSweet proteins. List the key classes of glycoproteins, their defining characteristics, and their biological functions.arrow_forwardDraw any pentapeptide. All C-O, C-N, and C-S bonds must be written out, as well as all N-H, S-H, and O-H atoms/bonds. Your peptide must include at least one amino acid from each of the major classes of amino acids (i.e. charged, polar, etc.). Circle each peptide bond in this peptide.arrow_forward
- Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Val, Met, Asp (2 equiv), Phe, Trp, Ile, Lys, and forms the following fragments when partially hydrolyzed with HCl: Ile-Asp-Phe, Lys-Met-Val-Trp, and Phe-Asp-Lys-Met. Trp Leu Phe Leu Val Lys Gly Tyr Xarrow_forwardLong explanations are not needed. Answers and brief descriptions would be enough. During the formation of the peptide bond which of the following takes place? a. Hydrogen atom is lost from its carboxyl group of one amino acid and a hydrogen atom is lost from the amino group of another amino acid. b. Hydrogen atom is lost from its carboxyl group of one amino acid and a hydroxyl group is lost from the amino group of another amino acid. c. Hydroxyl group is lost from its carboxyl group of one amino acid and a hydroxyl group is lost from the amino group of another amino acid. d. Hydroxyl group is lost from its carboxyl group of one amino acid and a hydrogen atom is lost from the amino group of another amino acid.arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Lys, Pro, Tyr, Ile (2 equiv) , Gln, Trp, Phe, and forms the following fragments when partially hydrolyzed with HCl: Lys–Ile-Phe-Pro, Phe-Pro-Gln-Tyr, and Trp-Ile-Lys.arrow_forward
- Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.arrow_forwardDo not give handwriting solution. Draw A mixed triacylglycerol that contains one saturated 8 - carbon fatty acid chain and two 6 - carbonfatty acid chains with 2 trans double bonds each.arrow_forwardThis is DNA. Locate the nitrogen bases (nitrogens are blue). Where are they located in the molecule?Locate the sugars and phosphates, and describe their location. Adjacent nucleotides are linked by covalent phosphodiester bonds (-O-P-O-) produced by a condensation reaction. What parts of the adjacent nucleotides are linked by phosphodiester bonds?Two nitrogenous bases extending towards the middle of the double helix. Are there any covalent bonds between these bases?If there are no covalent bonds between these bases, what other kinds of bonds might hold the two strands of the double helix together?arrow_forward
- Based. On the table explain the difference of net charge between 168.1 and the 168.10 molecular clones. Consider the initial net charge of the 168.1 clone and what ionizable amino acids contribute to such charge. Assume that histidine is neutral due to the pharrow_forwardLabel the horizontal axis. Consider two proteins: hexokinase has a pI ~ 4.5, and actin has a pI ~ 7.5. Draw a curve for each protein on the axes, indicating how the charge of the protein changes with the pH of the medium. Be sure to label which curve is which.arrow_forwardб. Draw all possible products of a single hydrolysis being completed on the following polypeptide: Ala-Ser-Met-Serarrow_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
![Text book image](https://www.bartleby.com/isbn_cover_images/9781319114671/9781319114671_smallCoverImage.jpg)
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
![Text book image](https://www.bartleby.com/isbn_cover_images/9781464126116/9781464126116_smallCoverImage.gif)
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
![Text book image](https://www.bartleby.com/isbn_cover_images/9781118918401/9781118918401_smallCoverImage.gif)
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305961135/9781305961135_smallCoverImage.gif)
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305577206/9781305577206_smallCoverImage.gif)
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
![Text book image](https://www.bartleby.com/isbn_cover_images/9780134015187/9780134015187_smallCoverImage.gif)
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY