Homework Answers
C. Since the given ph is 4 (low ph) the pantapeptide will move toward negative electode.
If the pH of the buffer is above the pI of the protein being run, the protein will migrate to the positive pole.
If the pH of the buffer is below the pI of the protein being run, the protein will migrate to the negative pole.
If the protein is run with a buffer pH that is equal to the pI, it will not migrate at all.
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c) You place your pentapeptide into a buffer with a pH=4. What direction will your pentapeptide...
#1) For the following pentapeptide (Where pH =1): a) What would the net charge be for...
#1) For the following pentapeptide (Where pH =1):
a) What would the net charge be for the following pH?
pH 0 =
pH 3 =
pH 5 =
pH 7 =
pH 10 =
pH 13 =
b) Calculate the pl of the pentapeptide. (Cysteine: pK1 = 1.96,
pK2 = 10.128) ( Glutamine: pK1 = 2.17 , pK2 = 9.13) (Arginine: pK1
= 2.17. pK2 = 9.04) (Leucine: pK1 = 2.36 , pK2 = 9.60)
c) If you were to...
The one-letter sequence is: WATER a) Draw the peptide (R-groups trans), indicating charges, in pr...
The one-letter sequence is: WATER
a) Draw the peptide (R-groups trans), indicating charges, in
predominant form found at pH = 0.
b) What is the isoelectric point?
c) What is the average charge on the population of peptide
macromolecules at pH = 2.2?
d) What is the average charge on the population of peptide
macromolecules at pH = 12.5?
TABLE 4.1 Amino Acid Alanine Arginine Asparagine Aspartic acid Cysteine....« Glutamic acid Glutamine Glycine Histidine Isoleucine Leucine Lysine … Methionine Phenylalanine...
Multiple choice] 1. The R-group CH₂C₆H₅ belongs to: a. Arginine b. Phenylalamine c. Cysteine d. Aspartic...
Multiple choice] 1. The R-group CH₂C₆H₅ belongs to: a. Arginine b. Phenylalamine c. Cysteine d. Aspartic acid 2. Choose the INCORRECT statement: a. Peptides are amino acids joined by a peptide bond. b. A protein is hydrolyzed to a mixture of ά-amino acids c. A tripeptide has three peptide bonds. d. An ά-amino acid is a carboxylic acid with an amine group on the ά carbon.
Question 6 (1 point) in the A pH versus rate curve with an inflection point at...
Question 6 (1 point) in the A pH versus rate curve with an inflection point at pH-4 suggests the involvement of an catalytic step Question 8 (1 point) Cellulose and glycogen are both structural polysaccharides proton donation that is mediated by a coenzyme True False free proton surrounded by a hydrophobic environment proton transfer with a pK close to 4 Question 9 (1 point) proton abstraction that requires a metal ion in close proximity The activity of lysozyme is greater...
just need help on 4 and 5 Proteins (For these questions, you may research online or...
just need help on 4 and 5
Proteins (For these questions, you may research online or from the prescribed text book to arrive at your answers), for each question, justify your answers through technical reasoning. (5 points each) I. What is the general structure of an α-amino acid? Give an overview of general properties of amino acids. Comment on the particular characteristics of some amino acids and explain what the reason for their particular behavior is. 2. Write the chemical...
Question #4 (10 points) - Mass spectroscopy Amino Acid Molecular Weight 89 174 133 146 137,...
Question #4 (10 points) - Mass spectroscopy Amino Acid Molecular Weight 89 174 133 146 137, 194 Alanine Arginine Aspartic acid Glutamic acid Glycine Lysine Proline Serine Tyrosine Valine 105 384 340 Hidal 146 115 105 181 117 146 Mass/charge (here the charge is -1, so it's just mass) Above is shown a mass spectroscopy for a peptide 5 amino acids long derived from a soluble protein. This 5 amino acid peptide represents a hydrophilic surface part of the protein...
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...
My answers are: Question 1: False Question 4: proton transfer with a pK close to 4...
My answers are:
Question 1: False
Question 4: proton transfer with a pK close to 4
Question 5: the active site contains an aspartic acid and
glutamic acid, both of which must be deprotonated
Question 8: 2 histidine residues with somewhat different pKa
values act as acids and bases during catalysis
Can someone please check my answers?
Question 1 (1 point) Cellulose and glycogen are both structural polysaccharides True False Question 4 (1 point) _ in the A pH versus...
Proteins (For these questions, you may research online or from the prescribed text book to arrive...
Proteins (For these questions, you may research online or from the prescribed text book to arrive at your answers), for each question, justify your answers through technical reasoning. (5 points each) I. What is the general structure of an α-amino acid? Give an overview of general properties of amino acids. Comment on the particular characteristics of some amino acids and explain what the reason for their particular behavior is. 2. Write the chemical formula of a peptide that consists of...
(1) The following diagram represents a titration curve of histidine as pH increases; pKa = 1.82 represents the terminal carboxylic acid group. pK, represents the terminal amino group: 6.0 r...
(1) The following diagram represents a titration curve of histidine as pH increases; pKa = 1.82 represents the terminal carboxylic acid group. pK, represents the terminal amino group: 6.0 represents the R-group, and pK, E 9.17 7.59 pH 182 3.0 20 10 H (equivalents) At what point on the diagram is histidine predominantly present as the following species? COO A, at pH < 1.82 B. between pH 1.82 and pH 6.0 C) between pH 6.0 and pH 9.17 D. at...
#1) For the following pentapeptide (Where pH =1):
a) What would the net charge be for the following pH?
pH 0 =
pH 3 =
pH 5 =
pH 7 =
pH 10 =
pH 13 =
b) Calculate the pl of the pentapeptide. (Cysteine: pK1 = 1.96,
pK2 = 10.128) ( Glutamine: pK1 = 2.17 , pK2 = 9.13) (Arginine: pK1
= 2.17. pK2 = 9.04) (Leucine: pK1 = 2.36 , pK2 = 9.60)
c) If you were to...
The one-letter sequence is: WATER
a) Draw the peptide (R-groups trans), indicating charges, in
predominant form found at pH = 0.
b) What is the isoelectric point?
c) What is the average charge on the population of peptide
macromolecules at pH = 2.2?
d) What is the average charge on the population of peptide
macromolecules at pH = 12.5?
TABLE 4.1 Amino Acid Alanine Arginine Asparagine Aspartic acid Cysteine....« Glutamic acid Glutamine Glycine Histidine Isoleucine Leucine Lysine … Methionine Phenylalanine...
Question 6 (1 point) in the A pH versus rate curve with an inflection point at pH-4 suggests the involvement of an catalytic step Question 8 (1 point) Cellulose and glycogen are both structural polysaccharides proton donation that is mediated by a coenzyme True False free proton surrounded by a hydrophobic environment proton transfer with a pK close to 4 Question 9 (1 point) proton abstraction that requires a metal ion in close proximity The activity of lysozyme is greater...
just need help on 4 and 5
Proteins (For these questions, you may research online or from the prescribed text book to arrive at your answers), for each question, justify your answers through technical reasoning. (5 points each) I. What is the general structure of an α-amino acid? Give an overview of general properties of amino acids. Comment on the particular characteristics of some amino acids and explain what the reason for their particular behavior is. 2. Write the chemical...
Question #4 (10 points) - Mass spectroscopy Amino Acid Molecular Weight 89 174 133 146 137, 194 Alanine Arginine Aspartic acid Glutamic acid Glycine Lysine Proline Serine Tyrosine Valine 105 384 340 Hidal 146 115 105 181 117 146 Mass/charge (here the charge is -1, so it's just mass) Above is shown a mass spectroscopy for a peptide 5 amino acids long derived from a soluble protein. This 5 amino acid peptide represents a hydrophilic surface part of the protein...
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...
My answers are:
Question 1: False
Question 4: proton transfer with a pK close to 4
Question 5: the active site contains an aspartic acid and
glutamic acid, both of which must be deprotonated
Question 8: 2 histidine residues with somewhat different pKa
values act as acids and bases during catalysis
Can someone please check my answers?
Question 1 (1 point) Cellulose and glycogen are both structural polysaccharides True False Question 4 (1 point) _ in the A pH versus...
Proteins (For these questions, you may research online or from the prescribed text book to arrive at your answers), for each question, justify your answers through technical reasoning. (5 points each) I. What is the general structure of an α-amino acid? Give an overview of general properties of amino acids. Comment on the particular characteristics of some amino acids and explain what the reason for their particular behavior is. 2. Write the chemical formula of a peptide that consists of...
(1) The following diagram represents a titration curve of histidine as pH increases; pKa = 1.82 represents the terminal carboxylic acid group. pK, represents the terminal amino group: 6.0 represents the R-group, and pK, E 9.17 7.59 pH 182 3.0 20 10 H (equivalents) At what point on the diagram is histidine predominantly present as the following species? COO A, at pH < 1.82 B. between pH 1.82 and pH 6.0 C) between pH 6.0 and pH 9.17 D. at...
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