Draw a structure for a peptide that gives Ala, Leu & Val on hydrolysis and fails to react with phenyl isothiocyanate. Mass spectrometry gives a molar mass of 283 for this peptide.Draw the predominant structure at pH 7 using the charge tools to adjust formal charges.You do not have to consider stereochemistry.You do not have to explicitly draw H atoms.• Do not include lone pairs in your answer. They will not be considered in the grading.85کرChemDoodleⓇルنے

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Answered: Draw a structure for a peptide that…

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.52P

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Draw a structure for a peptide that gives Ala, Leu & Val on hydrolysis and fails to react with phenyl isothiocyanate. Mass spectrometry gives a molar mass of 283 for this peptide. Draw the predominant structure at pH 7 using the charge tools to adjust formal charges.
Draw a structure for a peptide that gives Ala, Leu & Val on hydrolysis and fails to react with phenyl isothiocyanate. Mass spectrometry gives a molar mass of 283 for this peptide. Draw the predominant structure at pH 7 using the charge tools to adjust formal charges. • You do not have to consider stereochemistry. You do not have to explicitly draw H atoms. • Do not include lone pairs in your answei. opy aste ChemDoodle
I don't get it at all. Can you help me about the Henderson-Hasselbalch relation, summarized in the table below, it is possible to predict the predominant form of these groups at a particular pH? Draw the line bond structure for the general form of an amino acid using "R" to represent the side chain. Draw the N- and C-terminus groups using the forms that are predominant at physiological pH (pH = 7.4. Include lone pairs in your drawing.
13- If you were to have a mythical AA based on Aspartic acid in which the carboxylate on the side chain is replaced by a hydroxyl (alcoholic) group with pKa of 15.0. What would be the predominant form of this AA at pH 1, 7 and 12? Draw ALL structures with the correct net charges.
Modify the structures (if necessary) to show the predominant form of the amino acid tyrosine at each pH. Be sure to include the proper number of hydrogen atoms on heteroatoms and the correct formal charges on atoms. At pH 3.5 Select Draw Templates More 15 C H₂N - CH I CH₂ HC = || HN HC OH OH O CH CH ✔ Erase 2 Q At pH 13.0 Select Draw Templates More G ✔ ||| C H N H₂N HC HC CH | CH₂ OH OH O CH | CH Erase Q2 Q
(b) Describe how the charge of some amino groups in a protein might differ at pH 9.0 and pH 5.0. the charge on the amino group will differ at pH 5 and pH 9 which will depend on the pKa of the amino acid. (c) Describe how the charge of some carboxyl groups in a protein might differ at pH 9.0 and pH 5.0. charge on carboxyl group will differ at pH 5 and pH 9 which will depend on the pKa of the amino acid. (d) Given your answers to parts (b) and (c), what kind of intramolecular interactions in beta-galactosidase are most likely to be affected by a change in pH from 9.0 to 5.0? (e) Could the interactions you mention in part (d) affect the catalytic activity of beta-galactosidase?
The image below is a positive ionization mode Electrospray ionization-mass spectrum (ESI-MS) spectrum for a peptide, obtained using high resolution mass spectrometry. If ionization occurs through de-protonation (assuming that the mass of a proton is 1.0 Da), what is the neutral mass of the peptide, in Da? 627.271 627.604 100 - 627.938 628.271 628.604 628.938 627.0 628.0 629.0 mass/charge (m/z) 628.271 626.271 1878.813 O 1884.813 % Abundance
A chemically modified guanidino group is present in cimetidine (Tagamet), a widely prescribed drug for the control of gastric acidity and peptic ulcers. Cimetidine reduces gastric acid secretion by inhibiting the interaction of histamine with gastric H2 receptors. In the development of this drug, a cyano group was added to the substituted guanidino group to alter its basicity. Do you expect this modified guanidino group to be more basic or less basic than the guanidino group of arginine? Explain.
Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (-NH3), and the other for the carboxyl (-COOH) group. Therefore, it has two pKą values. The carboxyl group has a pK₁ of 2.34 and the a-amino group has a pK₂ of 9.60. Glycine can exist in fully deprotonated (NH₂-CH₂-COO-), fully protonated (NH3-CH₂-COOH), or zwitterionic form (NH3-CH₂-COO-). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of th pH. fully deprotonated form NH,−CH,−COO- pH 11.9 pH 6.0 pH 8.0 fully protonated form NH3-CH₂-COOH pH 1.0 Answer Bank pH 7.0 zwitterionic form NH3-CH₂-COO-
For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?apKa of 3.3. The amino group of alanine has a p?apKa of 8.8. Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7.
Chemistry Write structure for oligopeptides “Boc-CPID-benzyl ester” and “Methy ester-CGLK-Boc”. Also show all the possible types of bonding between the two peptide chains.
Draw a structural formula for the major ionic form of the amino acid shown below when in aqueous solution at pH 1.5. H₂NCCH₂CHCOH J *NH3 asparagine • You do not have to consider stereochemistry. You do not have to explicitly draw H atoms. • Do not include lone pairs in your answer. They will not be considered in the grading.

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