(a)
Interpretation:
The amino acid that would be more soluble in water needs to be identified.
Ala, Leu
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.
(b)
Interpretation:
The amino acid that would be more soluble in water needs to be identified.
Tyr, Phe
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.
(c)
Interpretation:
The amino acid that would be more soluble in water needs to be identified.
Ser, Ala
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.
(d)
Interpretation:
The amino acid that would be more soluble in water needs to be identified.
Trp, His
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.
![Check Mark](/static/check-mark.png)
Want to see the full answer?
Check out a sample textbook solution![Blurred answer](/static/blurred-answer.jpg)
Chapter 2 Solutions
BIOCHEMISTRY
- Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?arrow_forwardIdentify. Examine the following four amino acids (A-D): Co0 "H,N- CH "H,N CH "H;N-CH "H,N CH CH2 CH2 CH, CH CH2 CH3 CH, CH2 OH NH," B D What are their names, three-letter abbreviations, and one-letter symbols?arrow_forwardIonization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. 1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state? 2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently. 3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?arrow_forward
- Peptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?arrow_forward. 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.arrow_forwardAccepting. Which of the following compounds readily accepts amino groups from amino acids? a. Glutamine b. Isocitrate c. Malate d. a-Ketoglutarate-Ketoglutaratearrow_forward
- Please help me with this question. More than one answer may be correct. Elastin _______. Options: A) has a repeating structure of 3 amino acids such as Gly-Pro-X B) crosslinks with numerous other elastin peptides to make an elastic fiber C) is physically attached to the smooth endoplasmic reticulum D) is physically attached to ribosomes E) is rich in hydrophobic residuesarrow_forward. Provide an explanation for the fact that a-D-mannose is more stable than B-D-mannose, whereas the opposite is true for glucose.arrow_forwardcotton. Which aspect of the structure of cellulose accounts for its strength? Cellulose is an abundant structural polysaccharide found in plant cell walls, wood, and interchain hydrogen bonding between extended molecular chains repeating unit of N-acetylglucosamine a(1→4) linkages between glucose units branches that occur every 12-30 residues forms a helical conformation in water Which of the following is not correct about chitin? fundamental constituent of the exoskeletons of crustaceans, insects, and spiders b) chitin chains form extended ribbons that pack side-by side a) similar to cellulose but with repeating units of N-acetyl-D-glucosamine c) d) found mainly in the liver in humans, making up as much as 10% of liver mass stacked sheets of chitin strands are stabilized by intrastrand, interstrand, and intersheet hydrogen bondsarrow_forward
- More ratios. Through the use of nuclear magnetic resonance spectroscopy, it is possible to determine the ratio between the protonated and deprotonated forms of buffers. (a) Suppose the ratio of [ A- ]A I to [HA] is determined to be 0.1 for a buffer with pKar6.0.pKa = 6.0. What is the pH? (b) For a different buffer, 91974 suppose the ratio of [ A- ]lA J to [HA] is determined to be 0.1 and the pHpH is 7.0. In this case, what is the pKapKa of the buffer? (c) For another buffer with pKa=7.5PKa = 7.5 at pH 8.0pH 8.0, what is the expected ratio of [ A- ][A ] to [HA]? doarrow_forwardESSAY TYPE. Briefly describe how monosaccharides like glucose and fructose assume or transform into its corresponding Haworth structure.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
- 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)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781464126116/9781464126116_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781118918401/9781118918401_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305961135/9781305961135_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305577206/9781305577206_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9780134015187/9780134015187_smallCoverImage.gif)