2. Compare and contrast the biological roles of the following amino acids the following pairs of amino acids. Once you have documented these role state which member of the pair is most important and why (1-2 sentences) Pair #1 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Aspartic acid Glutamic acid Important in which pathways Pair #2 Arginine Histidine Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Pair #3 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Important in which pathways Tyrosine Phenylalanine

2. Compare and contrast the biological roles of the following amino acids the following pairs of amino acids. Once you have documented these role state which member of the pair is most important and why (1-2 sentences) Pair #1 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Aspartic acid Glutamic acid Important in which pathways Pair #2 Arginine Histidine Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Pair #3 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Important in which pathways Tyrosine Phenylalanine

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.57
a. The graph to the right displays the degree of helicity that was measured for a peptide as nine additional amino acids were sequentially added to the initial amino acid. Describe the reasons that the helicity curve takes the shape that it does as amino acids are added on to the small peptide.
None
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
Biochemistry，based on the example，need help to 1）hand draw the dipeptides that contains Glutamic acid and Proline. 2）hand draw the tetra peptides that contains Glycine ， Alanine，Glutamic acid and Proline.
The tripeptide +H3N-Leu-His-Glu-COO- has pKa values of 2.2, 3.6, 6.0 and 9.1. The isoelectric point (pI) for this peptide will be: 8 5 6 4 None of the above
Indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser none
Thank you very much for your assitance as it is greatly appreciated.
Consider the peptide HRDMQSGAI. Part: 0/5 Part 1 of 5 Identify the side chains of the amino acid residues in the peptide that are nonpolar. Check all that apply. H R D ☐ M 1Q S G None of the above x
Determine whether each of the amino acids is polar, nonpolar, positively charged, or negatively charged at pH 7. Polar and neutral aspartate H Ser H₂N-C-CH₂-C-COO NH3 lysine Leu Nonpolar Answer Bank H OOC-CH₂-CH₂-C-COO NH3 Positively charged H CH₂-C-COO NH3 hydrophobic amino acids Negatively charged
At which pH would the peptide with the amino acid sequence 'KEYHR' be found in an IPG (Immobilized pH gradient) strip after successful isoelectric focusing. Show calculation. lonizable groups Alpha amine group of K Side chain group of K Side chain group of E Side chain group of Y Side chain group of H Side chain group of R Alpha carboxylic acid group of R pka 8.95 10.53 4.25 10.07 6 12.48 2.17