Homework Answers
3.a) [i] The type of interaction occurring between Leucine and Phenylalanine at pH 7.4 is primarily hydrophobic interactions between the alkyl side chain of leucine and the bulky benzyl group of phenylalanine
[ii] Two cysteine molecules will interact to form a di-sulphide linkage and the resultant will be a cystine molecule.
[iii] Electrostatic interactions can occur between aspartate (which will have a negative charge at pH 7.4) and threonine's hydroxyl group.
[iv] Electrostatic interactions can occur between Aspartate and arginine at pH 7.4
b) Secondary and tertiary structures of amino acids are stabilised by interactions between amino acid side chains.
c) Two types of secondary structures are alpha helix and beta sheets.
In alpha helix, the side chains are placed out of the helix in a plane similar to that of the helix for the formation of stabilising bonds whereas in beta sheets the side chains are placed out of the structure but in a plane perpendicular to that of the beta-sheet plane.
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3) Protein structure and amino acid side chains a) Give examples of the types...
PLEASE HELP OCHEM QUESTION 1. In the following protein, identify the type of bonding or interaction...
PLEASE HELP OCHEM QUESTION
1. In the following protein, identify the type of bonding or interaction that is responsible for holding the two peptide chains together at each amino acid pair, above (A) and below (B). Gly - Ala - Ser - Cys - Val - Asp - Leu - Thr - His - Ile-Tyr-Glu - Phe - Lys - Cys - Met - Asn Val - Leu -Gin-Cys - Pro-Lys - Met - Tyr - Asp -Phe-Asn-Lys - Ile...
please explain how to solve this problem, the answer is provided 9. Peptides: (20 pts.). A...
please explain how to solve this problem, the answer
is provided
9. Peptides: (20 pts.). A polypeptide (X) gives 7 fragments when treated with chymotrypsin (A-G). The same peptide also gives 9 fragments when treated with trypsin (I- IX). After Chymotrypsin A) Thr-Thr-Tyr-Ala-Gly-Phe-Phe-Ile-Asp- Lys B) Ala-Cys-Pro-Leu-Tyr-Gin-lle-Arg C) Met-Ser-Thr-Tyr-Pro-Gly-Arg D) Cys-Leu-Val-Phe-Ile-Lys E) Leu-Ala-Trp-Gly-Val F) Ser-Phe-Ala-Pro-Lys G) Met-Asp-Lys Afier Trypsin I) Ala-Pro-Lys-Met-Asp-Lys-Thr-Thr-Tyr II) Pro-Gly-Arg-Cys-Leu-Val-Phe III) Ile-Lys-Ala-Cys-Pro-Leu-Tyr IV) Ile-Asp-Lys-Met-Ser-Thr-Tyr V) Gin-Ile-Arg-Leu-Ala-Trp VIAla-Gly-Phe VII) Gly-Val VIII) Ser-Phe LX) Phe A) What is the primary...
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...
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D....
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
Describe the four categories of amino acid side chains. What types of interactions are the members...
Describe the four categories of amino acid side chains. What types of interactions are the members of each of these categories likely to make? Now describe and explain the four levels of protein structure, giving a specific example of each an how amino acids are involved.
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...
anyone can help me with it? A protein biochemist attempted to determine the amino acid sequence...
anyone can help me with it?
A protein biochemist attempted to determine the amino acid sequence of a decapeptide. Use the results from the trypsin, chymotrypsin, and cyanogen bromide treatments to suggest the amino acid sequence of this decapeptide. Trypsin digestion gave two fragments with multiple residues (not in order): • T1: Ala, Arg, Phe, Gly, Thr, Trp, Tyr • T2: Lys, Met, Val Chymotrypsin digestion gave four fragments with multiple residues (not in order): • CT1: Ala, Phe •...
20. Protein amino acid side chains can hydrogen bond in the major groove of DNA, and...
20. Protein amino acid side chains can hydrogen bond in the major groove of DNA, and discriminate between each of the four possible base pairs. In which one of the following groups of amino acids can all three members potentially be used in such DNA-protein recognition? A) Ala, Asn, Glu B) Arg. Gin, Leu C) Asn, Gin, Trp D) Asn, Glu, Lys E) Glu, Lys, Pro 21. Compared with DNA polymerase, reverse transcriptase: A) does not require a primer to...
Identify the preferred orientation of amino acid side chains in the tertiary structure of a protein...
Identify the preferred orientation of amino acid side chains in the tertiary structure of a protein in an aqueous environment. A. The hydrophobic side chains will prefer to be on the interior where they can interact with water molecules in the aqueous environment. B. The hydrophilic side chains will prefer to be on the exterior where they can interact with water molecules in the aqueous environment. C. The hydrophilic side chains will prefer to be on the interior where they...
a. Using the table below, predict the secondary structure most likely adopted by the heptapeptide "RANGEHEAL". W...
a. Using the table below, predict the secondary structure most
likely adopted by the heptapeptide "RANGEHEAL". Will it be
alpha-helical, beta-strand, or just random coil?
b. Hydrogen bonds between backbone residues stabilize
interactions between
helixes and
sheets. Knowing this and other information about hydrogen bonds,
which amino acid from the picture below will destabilize secondary
protein structure?
Conformational Preferences of the Amino Acids Preference Amino acid a-helix B-strand Reverse turn Glu 1.59 0.52 1.01 Ala 1.41 0.72 0.82...
PLEASE HELP OCHEM QUESTION
1. In the following protein, identify the type of bonding or interaction that is responsible for holding the two peptide chains together at each amino acid pair, above (A) and below (B). Gly - Ala - Ser - Cys - Val - Asp - Leu - Thr - His - Ile-Tyr-Glu - Phe - Lys - Cys - Met - Asn Val - Leu -Gin-Cys - Pro-Lys - Met - Tyr - Asp -Phe-Asn-Lys - Ile...
please explain how to solve this problem, the answer
is provided
9. Peptides: (20 pts.). A polypeptide (X) gives 7 fragments when treated with chymotrypsin (A-G). The same peptide also gives 9 fragments when treated with trypsin (I- IX). After Chymotrypsin A) Thr-Thr-Tyr-Ala-Gly-Phe-Phe-Ile-Asp- Lys B) Ala-Cys-Pro-Leu-Tyr-Gin-lle-Arg C) Met-Ser-Thr-Tyr-Pro-Gly-Arg D) Cys-Leu-Val-Phe-Ile-Lys E) Leu-Ala-Trp-Gly-Val F) Ser-Phe-Ala-Pro-Lys G) Met-Asp-Lys Afier Trypsin I) Ala-Pro-Lys-Met-Asp-Lys-Thr-Thr-Tyr II) Pro-Gly-Arg-Cys-Leu-Val-Phe III) Ile-Lys-Ala-Cys-Pro-Leu-Tyr IV) Ile-Asp-Lys-Met-Ser-Thr-Tyr V) Gin-Ile-Arg-Leu-Ala-Trp VIAla-Gly-Phe VII) Gly-Val VIII) Ser-Phe LX) Phe A) What is the primary...
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...
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
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...
anyone can help me with it?
A protein biochemist attempted to determine the amino acid sequence of a decapeptide. Use the results from the trypsin, chymotrypsin, and cyanogen bromide treatments to suggest the amino acid sequence of this decapeptide. Trypsin digestion gave two fragments with multiple residues (not in order): • T1: Ala, Arg, Phe, Gly, Thr, Trp, Tyr • T2: Lys, Met, Val Chymotrypsin digestion gave four fragments with multiple residues (not in order): • CT1: Ala, Phe •...
20. Protein amino acid side chains can hydrogen bond in the major groove of DNA, and discriminate between each of the four possible base pairs. In which one of the following groups of amino acids can all three members potentially be used in such DNA-protein recognition? A) Ala, Asn, Glu B) Arg. Gin, Leu C) Asn, Gin, Trp D) Asn, Glu, Lys E) Glu, Lys, Pro 21. Compared with DNA polymerase, reverse transcriptase: A) does not require a primer to...
a. Using the table below, predict the secondary structure most
likely adopted by the heptapeptide "RANGEHEAL". Will it be
alpha-helical, beta-strand, or just random coil?
b. Hydrogen bonds between backbone residues stabilize
interactions between
helixes and
sheets. Knowing this and other information about hydrogen bonds,
which amino acid from the picture below will destabilize secondary
protein structure?
Conformational Preferences of the Amino Acids Preference Amino acid a-helix B-strand Reverse turn Glu 1.59 0.52 1.01 Ala 1.41 0.72 0.82...
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