Draw the two amino acids serine and alanine, and a dipeptide that could be formed by combining these two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature the amino terminus is on the left and the carboxyl terminus is on the right. 1. How many waters were released by formation of this dipeptide from individual amino acids? [ Select ] 2. How many hydrogen bond donors does your dipeptide have? [ Select ] 3. If you were to draw this dipeptide at a pH = 1, would the number of hydrogen bond donors change? [ Select ]
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- Draw the two amino acids serine and alanine, and a dipeptide that could be formed by combining these two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature the amino terminus is on the left and the carboxyl terminus is on the right. 1. How many waters were released by formation of this dipeptide from individual amino acids? two 2. How many hydrogen bond donors does your dipeptide have? 2 3. If you were to draw this dipeptide at a pH = 1, would the number of hydrogen bond donors change? yes, the number of H-bond1. Draw an approximate titration curve of the following amino acid. Label the approximate isoelectric point of arginine on the curve and be sure to label the axis of the graph appropriately. You DO NOT need to draw the structure of this amino acid here. Pk1= 1.92, pk2=8.99 and pk3=12.48. Show your work for determining the isoelectric point. You can draw out your curve within the text box or upload a drawing. A▾ B I - I B 7A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
- Shown below are three amino acids: H,N-CH-C-o ҫн, H,N-CH-C-o CH, H,N-CH-C-o ČH, Tyrosine Tyr Y Phenylalanine Phe F Alanine Ala A 1. Which amino acid is the least hydrophobic? 2. Which amino acid is most hydrophobic? 3. Which amino acid is intermediate? 4. Explain why (2) is more hydrophobic than (3). 5. Explain why (3) is more hydrophobic than (1).Refer to following peptide structure: H&N CH3 IZ CH3- CH₂OH IZ OH ZI CH3 CH3. OH IZ OH IZ CH2 CONH2 parce 0 IZ Calculate the net charge of this peptide at pH = 12. OH CH3 What is the identity of the second residue in the peptide shown below? Enter the capitalized single letter abbreviation. 0- Estimate the pl and round to the nearest whole number. Use pKa values provided in lecture.Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZI
- The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 1? Type your answer... ints The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 7? Type your answer... The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 15? Type your answer... The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the isoelectric point of this peptide? Type your answer... SubmitDraw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0 backbone of glutamic acid. 2. Ionic bond- between ionized aspartic and asparagine amino acids. 3. Disulfide interaction between 2 molecules of Cysteine amino acids. 4. Hydrophobic interaction between Alanine and Leucine R-groups.The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 1? Type your answer... ints The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 7? Type your answer... 14- The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the isoelectric point of this peptide? Type your answer... -- - The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 15? Type your answer... --D Submit
- 2) Suppose you have a peptide composed of 4 amino acids bonded together: alanine, arginine, asparagine, and the novel amino acid armadillamine, which has an ionizable side group with a pKa of 7.2. At pH 9.5, this peptide has a net charge of -1. What is the charge on the protonated form of the armadillamine side group? Explain how you determined the charge on the protonated armadillamine side group)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 9.571. What will happen if there is a change in the configuration of a protein molecule? Provide an example. 2. Give the IUPAC name for Ala-Gly-Leu