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* Question Completion Status: QUESTION 5 Look at the structures of the following amino acids. Identify...
Identify the structure of amino acids, and describe the process by which they join together to...
Identify the structure of amino acids, and describe the process by which they join together to form polypeptides. Describe the 4 different groups of amino acids and their properties (Neutral, Polar, Acidic, Basic). Describe the levels of structure of proteins (primary, secondary, tertiary, and quaternary), including what bonds and interactions occur at EACH level. Describe denaturation of a protein and indicate how temperature and pH affect the protein functions. Describe the major functions of proteins
(a) Identify all the amino acids from the structures below and use these structures to describe...
(a) Identify all the amino acids from the structures below and use these structures to describe the meaning of the following in terms of protein structure; i. an intramolecular disulphide bond, "hydrophobic interaction”, iii. pH dependent electrostatic forces. а) соон yoon с) соон H.N—C—H H.N— C—H HNg–H | d) соон H,N—C—H CH2 SH CH, CH (b) Describe the process of protein denaturation and explain why high temperatures promote denaturation. Include a description of the role of protein denaturation in the...
Please explain, Thanks! The following image shows the 20 amino acids found in proteins. OH CH...
Please explain, Thanks!
The following image shows the 20 amino acids found in proteins. OH CH H HNCOOH Glycine HN HẠN CHO Alanine HẠN COOH Serine н соон Threonine Cysteine HAN COOHHN COOH Nлсоон н соон Methionine Valine Leucine Isoleucine Proline OOH MNCOOHHN COOH HN COOH H COOH HẠNỐIOOH Apartic Acid Phenylalanine Tyrosine Tryptophan Glutamic Acid HNCOOHH COOH Asparagine Glutamine HNCOOHNCOOH Histidine Lysine н соон Arginine Imagine that in a protein, a lysine amino acid is replaced with an isoleucine....
Identify the structural components of an amino acid and understand the chemical diversity of amino acids...
Identify the structural components of an amino acid and understand the chemical diversity of amino acids Question Coo- Anch H₂N-CH2 H2C CH Proline Proline's structure has a unique feature not found in other amino acids. What is it? Select the correct answer below: O Proline is chiral. O The amino group is part of the side chain. O Proline is positively charged. O Proline is achiral. P FEEDBACK MORE INSTRUCTION SUBMIT Content attribution Understand protonation and deprotonation of carboxyl and...
Question 1 (0.5 points) Saved Proteins are formed by joining together. carboxylic acids fatty acids amino...
Question 1 (0.5 points) Saved Proteins are formed by joining together. carboxylic acids fatty acids amino acids none of the above Question 2 (0.5 points) Which two functional groups does an amino acid contain? amine and carboxylic acid carboxylic acid and amide amide and heterocyclic ring heterocyclic ring and amine Question 3 (0.5 points) Do amino acids commonly exist in nature as neutral molecules with all uncharged atoms? Yes No Question 1 (0.5 points) What is a protein? A polymer...
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...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid an...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid and serine, whose structures are shown here, is HiN-CH-C-0HIN-CH-C-0 CH2 CH OH aspartic acid serine A HN-CH-C-o-N-CH-C-o CH OH CH2 coo -(H-C-o-H-c-o CH OH CH2 HIN CH-C-N-CH-C-O CH OH CH H-CH-CH CH CH OH coo- 20) Where is the peptide bond located in this dipeptide? serine valine a) the CO-NH joining serine and the valine b) the doubly bonded oxygen just left of center between the...
Consider the following amino acids for questions 11-13. Choose the best answers. cysteine serine lysine phenylalanine...
Consider the following amino acids for questions 11-13. Choose the best answers. cysteine serine lysine phenylalanine aspartate Which amino acid's R group has a pKa nearest physiological pH? Which amino acid would you most expect to find in the centre of a folded globular protein? Which amino amino acid can be phosphorylated? The overall charge on the peptide (G-R-A-M-P-S) at pH 12.5 is: -1 -0.5 -1.5 +0.5 1 15. What term best describes the protein secondary structure element drawn below:...
Question 24 Refer to the table below to answer the following question. А G U Serine...
Question 24 Refer to the table below to answer the following question. А G U Serine Serine Serine U с A UAA U с А с w Phenylalanine UCU UUC Phenylalanine UCC UUA Leucine UCA UUG Leucine UCG CUU Leucine CCU CUC Leucine сос CUA Leucine CCA CUG Leucine CCG Isoleucine ACU AUC Isoleucine ACC AUA Isoleucine ACA AUG Methionine Start ACG GUU Valine GCU GUC Valine GCC GUA Valine GCA GUG Valine GCG UAU Tyrosine UAC Tyrosine Stop UAG...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more likely to be found in these structures based on its charge and R-group size? A. Glycine B. Proline C. A sequence of several Glutamate D. A sequence of several Lysine E. Alanine Question 12. Which of the following is least likely to result in protein denaturation? A) Altering net charge by changing pH B) Changing the salt concentration C) Disruption of weak interactions by...
(a) Identify all the amino acids from the structures below and use these structures to describe the meaning of the following in terms of protein structure; i. an intramolecular disulphide bond, "hydrophobic interaction”, iii. pH dependent electrostatic forces. а) соон yoon с) соон H.N—C—H H.N— C—H HNg–H | d) соон H,N—C—H CH2 SH CH, CH (b) Describe the process of protein denaturation and explain why high temperatures promote denaturation. Include a description of the role of protein denaturation in the...
Please explain, Thanks!
The following image shows the 20 amino acids found in proteins. OH CH H HNCOOH Glycine HN HẠN CHO Alanine HẠN COOH Serine н соон Threonine Cysteine HAN COOHHN COOH Nлсоон н соон Methionine Valine Leucine Isoleucine Proline OOH MNCOOHHN COOH HN COOH H COOH HẠNỐIOOH Apartic Acid Phenylalanine Tyrosine Tryptophan Glutamic Acid HNCOOHH COOH Asparagine Glutamine HNCOOHNCOOH Histidine Lysine н соон Arginine Imagine that in a protein, a lysine amino acid is replaced with an isoleucine....
Identify the structural components of an amino acid and understand the chemical diversity of amino acids Question Coo- Anch H₂N-CH2 H2C CH Proline Proline's structure has a unique feature not found in other amino acids. What is it? Select the correct answer below: O Proline is chiral. O The amino group is part of the side chain. O Proline is positively charged. O Proline is achiral. P FEEDBACK MORE INSTRUCTION SUBMIT Content attribution Understand protonation and deprotonation of carboxyl and...
Question 1 (0.5 points) Saved Proteins are formed by joining together. carboxylic acids fatty acids amino acids none of the above Question 2 (0.5 points) Which two functional groups does an amino acid contain? amine and carboxylic acid carboxylic acid and amide amide and heterocyclic ring heterocyclic ring and amine Question 3 (0.5 points) Do amino acids commonly exist in nature as neutral molecules with all uncharged atoms? Yes No Question 1 (0.5 points) What is a protein? A polymer...
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...
19) The form of dipeptide aspatylserine (Asp-Ser) obtained from two amino acids, aspartic acid and serine, whose structures are shown here, is HiN-CH-C-0HIN-CH-C-0 CH2 CH OH aspartic acid serine A HN-CH-C-o-N-CH-C-o CH OH CH2 coo -(H-C-o-H-c-o CH OH CH2 HIN CH-C-N-CH-C-O CH OH CH H-CH-CH CH CH OH coo- 20) Where is the peptide bond located in this dipeptide? serine valine a) the CO-NH joining serine and the valine b) the doubly bonded oxygen just left of center between the...
Consider the following amino acids for questions 11-13. Choose the best answers. cysteine serine lysine phenylalanine aspartate Which amino acid's R group has a pKa nearest physiological pH? Which amino acid would you most expect to find in the centre of a folded globular protein? Which amino amino acid can be phosphorylated? The overall charge on the peptide (G-R-A-M-P-S) at pH 12.5 is: -1 -0.5 -1.5 +0.5 1 15. What term best describes the protein secondary structure element drawn below:...
Question 24 Refer to the table below to answer the following question. А G U Serine Serine Serine U с A UAA U с А с w Phenylalanine UCU UUC Phenylalanine UCC UUA Leucine UCA UUG Leucine UCG CUU Leucine CCU CUC Leucine сос CUA Leucine CCA CUG Leucine CCG Isoleucine ACU AUC Isoleucine ACC AUA Isoleucine ACA AUG Methionine Start ACG GUU Valine GCU GUC Valine GCC GUA Valine GCA GUG Valine GCG UAU Tyrosine UAC Tyrosine Stop UAG...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more likely to be found in these structures based on its charge and R-group size? A. Glycine B. Proline C. A sequence of several Glutamate D. A sequence of several Lysine E. Alanine Question 12. Which of the following is least likely to result in protein denaturation? A) Altering net charge by changing pH B) Changing the salt concentration C) Disruption of weak interactions by...
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