(a)
Interpretation:
The effect of the given environmental change on the
Concept introduction:
The organic compounds that contain
The value which determines the strength of an acid is known as
(b)
Interpretation:
The effect of the given environmental change on the
Concept introduction:
The organic compounds that contain amine
The value which determines the strength of an acid is known as
(c)
Interpretation:
The effect of the given environmental change on the
Concept introduction:
The organic compounds that contain amine
The value which determines the strength of an acid is known as
Want to see the full answer?
Check out a sample textbook solution- Required partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterinarrow_forwardMore 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_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
- . 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_forwardPeptides. 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_forwardNo plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.arrow_forward
- What else? What are cofactors? Carboxypeptidase requires a Zn²+ cofactor for the hydrolysis of the peptide bond of a C-terminal aromatic amino acid. T/F This is a structure of vitamin A. Is it polar or non polar? Explain OH Identify the following are water soluble or fat- soluble vitamins? HO H₂ H₂C H₂C H CH₂ H₂C HO. CH₂ OH CH₂ CH₂ CH3 O H 3) vitamin K 5) ascorbic acid OH HO D. vision E. blood clotting HỌ HO 10 OH Identify the vitamin associated with each of the following: 1) riboflavin (B2) 2) vitamin A 4) vitamin D 3 A. collagen formation B. part of the coenzymes FAD and FMN C. absorption of phosphorus and calcium in bone Make your own 3 questions with answers.arrow_forwarddisease. As such, a frontline treatment for Type 2 diabetes is the drug metformin, which acts indirectly to inhibit gluconeogenesis in the liver. You are a research biochemist who would like to develop new drugs that act to directly inhibit gluconeogenesis. You have just gained access to a library of thousands of small molecules of unknown activity, and you would like to identify lead compounds that have specific inhibitory activity against steps in the gluconeogenesis pathway. (a) into PEP in order to screen for inhibitors of enzymes specific to gluconeogenesis. Which enzymes do you need to purify, what cofactors and allosteric effectors do they require, and which reactants do you need to add to reconstitute the reactions for the first bypass? Which intermediates and products are generated? Your first approach is to reconstitute the initial set of bypass reactions that convert pyruvate (b) vitro reconstitution? What additional steps and enzymes are required in liver cells but are…arrow_forwardV-A. Which of the following amino acids will elute first in a cation-exchange column using a buffer at pH 7? 1. Asp or Lys 2. Arg or Met 3. Gly or Val 4. Ser or Alaarrow_forward
- Activity (% Max.) Using your knowledge of aspartyl proteases, develop a plausible explanation for why protein activity changes when pH is increased or decreased from pH 4, as shown in the graph. 06 08 09 10+ 4. 9. Hd Which statements are true? The protein is active when one asp residue is protonated and the other is deprotonated. O Both asp residues are protonated at more basic pH values. O Active aspartyl proteases have only one asp residue in the active site. Only one asp side chain is protonated at low pH (below pH 3.5). Both asp side chains are deprotonated at higher pH values.arrow_forwardmolecule. Which of the following fatty acids is an omega-3 fatty acid? bond starting with the third carbon from the methyl end (the omega end) of the Omega-3 (@-3) fatty acids are unsaturated fatty acids with a carbon-to-carbon double a-linolenic a) b) stearic oleic linoleic myristic ebil The molecule at the left is an example of which lipid? CH2 a) b) wax terpene steroid CH2 -0-P-0- d) sphingolipid glycerophospholipid bigit nisrtarrow_forwardNeed help. (a) Two ligands bind to the same site of a protein. However, when examined by ITC, for one of the ligands heat needs to be added to the system to maintain constant temperature, whereas for the other ligand, heat must be removed. Why is this the case?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