Homework Answers
Here two
neutral (Aliphatic and aromatic), Acidic and basic amino acids are
considered.
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CHM 230 F'19 Amino acids/peptides Worksheet 1. Draw the structure, at pH 7, of a tetrapeptide...
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an...
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an amide backbone. Although this amide backbone is common to all peptides, the so- called 'side-chan' groups attached to this backbone vary depending the amino acids used in the condensation reaction. Shown below are four different tetrapeptides (so-named because they are the products of the condensation of four amino acids). Based on their structures, predict the order of elution that one might expect if separating...
1. What amino acids do the following abbreviations stand for? Draw the structure of each. a)...
1. What amino acids do the following abbreviations stand for? Draw the structure of each. a) lle b) Thr c) Gin 2. Name and draw the structures of the amino acids that fit these descriptions: a) Contains an isopropyl group b) Contains a secondary alcohol group 3. Which of the following objects is chiral? a) A pair of scissors b) A comb c) A drinking glass 4. What does the term achiral mean? Give two examples involving organic structures.. 5....
Draw a peptide of two or more different amino acids. Circle the R group of each...
Draw a peptide of two or more different amino acids. Circle the R group of each amino acid. Put a box around each peptide bond. Identify each amino acid with the one-letter code.
(a) Draw three different amino acid residues connected by two peptide bonds. (b) label each residue...
(a) Draw three different amino acid residues connected by two peptide bonds. (b) label each residue (3-letter code is OK). (c) Note bonds that do not rotate with a star (d) Note bonds that do rotate with a semi-circle arrow, including those found in each side chain (e) Of the residues in your drawing, which one contributes most to the entropy of the polypeptide (assume an unfolded state)?
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...
12. Below is a portion of the abstract of a journal article. It describes the isolation,...
12. Below is a portion of the abstract of a journal article. It describes the isolation, purification, and determination of the peptide sequence as well as, the location of each of the disulfide bridges of an antibacterial peptide from the cowpea plant. Give brief and to the point answers to the questions based upon this information. (2 pts) FEBS Joumal 273 (2006) 3489-3497 2006 The Authors Journal compilation2006 FEBS Identification of a cowpea y-thionin with bactericidal activity Octávio L. Franco,...
s smı peptdes and ultimately proteins through a condensation fatt similar to the reactions that form...
s smı peptdes and ultimately proteins through a condensation fatt similar to the reactions that form a triglyceride from glycerol Amino acids combine to form peptides an protonated aater molecule is removed when a carboxylate and and three fatty acids. One and thretis amine react. Figure 1: o- HI Carboxylate reacts with Protonated Amide forming amine 2. Consider the two amino acids, tryptophan and serine bonds can be formed between these acids? How many different peptide 3. Draw each of...
Homework #11 (5 points) 1. Draw two amino acids. Circle around the carboxyl ends. Put a...
Homework #11 (5 points) 1. Draw two amino acids. Circle around the carboxyl ends. Put a double line und and the three-letter abbreviation for each amino acid. two amino acids. Circle the central carbon atoms. Underline the amino ends. Carboxyl ends. Put a double line under the R groups/ side chains. Write the name 2. How do enzymes increase the rate of chemical reactions? 3. What type of bond joins two amino acids together? 4. What are the three types...
The chemical structures of the 20 standard amino acids at pH 7, along with their 3...
The chemical structures of the 20 standard amino acids at pH 7, along with their 3 and 1 letter codes, are givern in alphabetical order below. While the oxygen and nitrogen atoms of the peptide bonds may serve as a donor atom to complex a metal ion, very often the ligands for the metal come from the amino acid side chains. Takea few moments to examine the chemical structures of the different side chains. Circle the side chains that you...
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an amide backbone. Although this amide backbone is common to all peptides, the so- called 'side-chan' groups attached to this backbone vary depending the amino acids used in the condensation reaction. Shown below are four different tetrapeptides (so-named because they are the products of the condensation of four amino acids). Based on their structures, predict the order of elution that one might expect if separating...
1. What amino acids do the following abbreviations stand for? Draw the structure of each. a) lle b) Thr c) Gin 2. Name and draw the structures of the amino acids that fit these descriptions: a) Contains an isopropyl group b) Contains a secondary alcohol group 3. Which of the following objects is chiral? a) A pair of scissors b) A comb c) A drinking glass 4. What does the term achiral mean? Give two examples involving organic structures.. 5....
(a) Draw three different amino acid residues connected by two peptide bonds. (b) label each residue (3-letter code is OK). (c) Note bonds that do not rotate with a star (d) Note bonds that do rotate with a semi-circle arrow, including those found in each side chain (e) Of the residues in your drawing, which one contributes most to the entropy of the polypeptide (assume an unfolded state)?
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...
12. Below is a portion of the abstract of a journal article. It describes the isolation, purification, and determination of the peptide sequence as well as, the location of each of the disulfide bridges of an antibacterial peptide from the cowpea plant. Give brief and to the point answers to the questions based upon this information. (2 pts) FEBS Joumal 273 (2006) 3489-3497 2006 The Authors Journal compilation2006 FEBS Identification of a cowpea y-thionin with bactericidal activity Octávio L. Franco,...
s smı peptdes and ultimately proteins through a condensation fatt similar to the reactions that form a triglyceride from glycerol Amino acids combine to form peptides an protonated aater molecule is removed when a carboxylate and and three fatty acids. One and thretis amine react. Figure 1: o- HI Carboxylate reacts with Protonated Amide forming amine 2. Consider the two amino acids, tryptophan and serine bonds can be formed between these acids? How many different peptide 3. Draw each of...
Homework #11 (5 points) 1. Draw two amino acids. Circle around the carboxyl ends. Put a double line und and the three-letter abbreviation for each amino acid. two amino acids. Circle the central carbon atoms. Underline the amino ends. Carboxyl ends. Put a double line under the R groups/ side chains. Write the name 2. How do enzymes increase the rate of chemical reactions? 3. What type of bond joins two amino acids together? 4. What are the three types...
The chemical structures of the 20 standard amino acids at pH 7, along with their 3 and 1 letter codes, are givern in alphabetical order below. While the oxygen and nitrogen atoms of the peptide bonds may serve as a donor atom to complex a metal ion, very often the ligands for the metal come from the amino acid side chains. Takea few moments to examine the chemical structures of the different side chains. Circle the side chains that you...
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