Draw the molecular structure of a tripeptide chain. Indicate which amino acid was added first (assuming...
Draw the molecular structure of a tripeptide chain. Indicate which amino acid was added first (assuming it was translated by a ribosome) by numbering the R groups as R1, R2, and R3 (you do not need to draw the structures of actual R groups for specific amino acids).
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Draw the molecular structure of a tripeptide chain. Indicate
which amino acid was added first (assuming...
2. The structure of the solid phase Wang resin linker and the first amino acid that we will use i...
2. The structure of the solid phase Wang resin linker and the first amino acid that we will use in this lab is shown below Fmoc first amino acid linker a) (1 pt) If the resin has 0.72 mmol/g of this linker on the surface of the beads, and you use 300 mg of resin for the reaction, how many mmol of linker do you have? b) (3 pts) All peptides will use alanine at the C-tenminus (position 1), Fmoc-L-valine...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptid...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptide that forms between serine and alanine. The dipeptide sequence is Ser-Ala. Label the peptide bond. 3.) How many amino acids residues are in a polypeptide containing 6 peptide bonds? How many peptide bonds are in a tripeptide 4.) Sketch a alpha-helix and a beta-sheet as best as you can. Label each.
1. a. For the following groups, indicate their predominant ionic species (draw the chemical structure) at...
1. a. For the following groups, indicate their predominant ionic species (draw the chemical structure) at pH 7.4: a. The side chain amino group (–NH3+) of the amino acid lysine, pKa=10.5. The side chain carboxyl group (-COOH) of the amino acid glutamate, pKa=4.1. b.For a buffer with a pKa of 8.03 : How will the pH and buffering capacity change when HCl is added to the buffer in “a”? How will the pH and buffering capacity change when NaOH is...
Question 5 Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has...
Question 5
Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...
Amino Acids SW C2 9. Which of the following is an L-amino acid? çoo coo coo...
Amino Acids SW C2 9. Which of the following is an L-amino acid? çoo coo coo HẠN |-R HANH, HẠN –H HÀNH R coo B. 10. The following questions refer to the structures A-E below: (a) Which represents the structure of an amino acid at very high pH? (b) Which is a zwitterion? (c) Which represents the structure of an amino acid at very low pH? (d) Which structure/(s) is/are) not possible? R-CH-COOR-CH-COOH R-CH-COOH R-CH-COOR -CH-COO NH2 NH2 *NH NH2...
a) which amino acid tested is most polar? b) look up the structure of the amino...
a) which amino acid tested is most polar?
b) look up the structure of the amino acids. explain why it
makes sense that the amino acid you listed is more polar than the
others?
c) what amino acids are in the fruit juice?
D. CHROMATOGRAPHY Chromatography is a general technique that is used to separate various materials. In this case, students can use the unique chemistry of the amino acid to determine its migration in a specific solvent. The solutions...
6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereoce...
6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereocentre). (b) What is the significance of chirality in the biological world? 7. (a) Sh (a) Show the repeating unit of the polypeptide chain in a protein and indicate the peptide bond. (b) What are the following structures of a protein (i) primary, (ii) secondary, (iii) tertiary and (iv) quaternary. 1. Polypeptides are the natural polymer of the naturally...
PRELAB ASSIGNMENT 1 Draw the structure of the amino acid son CH-OH Label the alpha carbon...
PRELAB ASSIGNMENT 1 Draw the structure of the amino acid son CH-OH Label the alpha carbon acid Sorine (en) which has R MO CHE OH CH2 OH 2. Draw the dipeptide that forms betw the peptide bond. s between serine and alanine The dipeptide sequence is Ser Ala Lace CH NCH H, A - — сH — с CH2 OH 3. How many amino aci arty amino acid residues are in a polypeptide containing 6 peptide bonos How many peptide...
Model 1 for reference, draw the structure of the given amino acid as it nly exist under each of t...
Model 1 for reference, draw the structure of the given amino acid as it nly exist under each of the following conditions for 1g.using Table 1 in a. valine; in the stomach at PH 1.5 Serine; in the small intestine at pH 10 c. Glutamate; in the blood plasma at pH 7.4 Information: Isoelectric points As shown in Model 3, amino acids do not normally exist in unionized forms. When an aminc acd contains both a (+) and a ()...
1) 2-amino-3-hydroxybutanoic acid 2) 2,3-dinitrobutane A. Draw the skeletal structure (line-bond) for the following compounds. B....
1) 2-amino-3-hydroxybutanoic acid
2) 2,3-dinitrobutane
A. Draw the skeletal structure (line-bond) for the following compounds. B. Convert the structures to the Most Stable and the Least Stable Newmann projections around (looking down) C2-C3 bond. (The numbering is based on the nomenclature locator numbers) C. On your skeletal structures, label the stereogenic centers (chiral carbons) if there are any. D. Draw all the possible stereoisomers for the compounds. Indicate which are enantiomer pairs. which are diastereomers to each other, and if...
2. The structure of the solid phase Wang resin linker and the first amino acid that we will use in this lab is shown below Fmoc first amino acid linker a) (1 pt) If the resin has 0.72 mmol/g of this linker on the surface of the beads, and you use 300 mg of resin for the reaction, how many mmol of linker do you have? b) (3 pts) All peptides will use alanine at the C-tenminus (position 1), Fmoc-L-valine...
Question 5
Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...
Amino Acids SW C2 9. Which of the following is an L-amino acid? çoo coo coo HẠN |-R HANH, HẠN –H HÀNH R coo B. 10. The following questions refer to the structures A-E below: (a) Which represents the structure of an amino acid at very high pH? (b) Which is a zwitterion? (c) Which represents the structure of an amino acid at very low pH? (d) Which structure/(s) is/are) not possible? R-CH-COOR-CH-COOH R-CH-COOH R-CH-COOR -CH-COO NH2 NH2 *NH NH2...
a) which amino acid tested is most polar?
b) look up the structure of the amino acids. explain why it
makes sense that the amino acid you listed is more polar than the
others?
c) what amino acids are in the fruit juice?
D. CHROMATOGRAPHY Chromatography is a general technique that is used to separate various materials. In this case, students can use the unique chemistry of the amino acid to determine its migration in a specific solvent. The solutions...
6. (a) Show the arrangement of the groups on the a carbon of the naturally occurring amino acids (draw out the stereocentre). (b) What is the significance of chirality in the biological world? 7. (a) Sh (a) Show the repeating unit of the polypeptide chain in a protein and indicate the peptide bond. (b) What are the following structures of a protein (i) primary, (ii) secondary, (iii) tertiary and (iv) quaternary. 1. Polypeptides are the natural polymer of the naturally...
PRELAB ASSIGNMENT 1 Draw the structure of the amino acid son CH-OH Label the alpha carbon acid Sorine (en) which has R MO CHE OH CH2 OH 2. Draw the dipeptide that forms betw the peptide bond. s between serine and alanine The dipeptide sequence is Ser Ala Lace CH NCH H, A - — сH — с CH2 OH 3. How many amino aci arty amino acid residues are in a polypeptide containing 6 peptide bonos How many peptide...
Model 1 for reference, draw the structure of the given amino acid as it nly exist under each of the following conditions for 1g.using Table 1 in a. valine; in the stomach at PH 1.5 Serine; in the small intestine at pH 10 c. Glutamate; in the blood plasma at pH 7.4 Information: Isoelectric points As shown in Model 3, amino acids do not normally exist in unionized forms. When an aminc acd contains both a (+) and a ()...
1) 2-amino-3-hydroxybutanoic acid
2) 2,3-dinitrobutane
A. Draw the skeletal structure (line-bond) for the following compounds. B. Convert the structures to the Most Stable and the Least Stable Newmann projections around (looking down) C2-C3 bond. (The numbering is based on the nomenclature locator numbers) C. On your skeletal structures, label the stereogenic centers (chiral carbons) if there are any. D. Draw all the possible stereoisomers for the compounds. Indicate which are enantiomer pairs. which are diastereomers to each other, and if...
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