An unknown amino acid found in some proteins has an R group with the structure —(CH2)3—XH...
An unknown amino acid found in some proteins has an R group with the
structure —(CH2)3—XH and its pKa= 8.5. In an aqueous solution, pH = 7.0, the residue would:
- exist in conjugate base form.
- exist in conjugate acid form.
- have charge of -1.
- have a charge of zero
- both a and c
- both a and d
- both b and d
Homework Answers
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An unknown amino acid found in some
proteins has an R group with the
structure
—(CH2)3—XH...
Lecture 3 Identify amino-/carboxy termini, and R-group on amino acid What is chirality? Identify a carbon...
Lecture 3 Identify amino-/carboxy termini, and R-group on amino acid What is chirality? Identify a carbon that is chiral (i.e., has 4 different groups attached) Chiral compounds rotate plane polarized light Memorize amino acid 1) structure, 2) classification (hydrophobic, aliphatic, aromatic, negatively charged, positively charged, polar uncharged) Be able to draw glycine (the generic amino acid) Given an amino acid structure and pKas of ionizable groups, be able to determine the charge at pH 1, pH 14, and pH 7...
of alanine has a pk of 9.87. What is the 153, The amino group charge on...
of alanine has a pk of 9.87. What is the 153, The amino group charge on that amino group at pH 7.0 145. Which amino acid serves as the first amino acid at the hN terminus of a newly synthesized protein? (B) methionine (A) alanine 9.80. The side chain of that amino acid includes (A) an amine group (C) a carboxylic acid group. (D) an alcohol 154. A certain amino acid has a pl (or pH, isoelectric point) (D) threonine...
20. In most proteins this amino acid's side chain is found clustered away from the aqueous...
20. In most proteins this amino acid's side chain is found
clustered away from the aqueous exterior of the protein as a result
of which interaction?
a) Hydrophobic effect
b) Charge-charge (ionic)
c) Dipole-dipole
d) Van der Waals (dispersion)
A protein has a pI of 6.5. If I want to use an anion exchange
resin (there is a +ve charge on the resin) to bind the protein,
what pH could I perform the separation at?
a) pH 8
b) pH...
Suppose you have a peptide composed of 4 amino acids bonded together: glutamine, glycine, glutamic acid,...
Suppose you have a peptide composed of 4 amino acids bonded together: glutamine, glycine, glutamic acid, and the novel amino acid friendsamine, which has an ionizable side group with a pKa of 5.9. At pH 7.0, this peptide has a net charge of -2. What is the charge on the protonated form of the friendsamine side group? Explain how you determined the charge on the protonated friendsamine side group
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...
20. Properties of a Buffer The amino acid glycine is often used as the main ingredient...
20. Properties of a Buffer The amino acid glycine is often used as the main ingredient of a buffer in biochemical experi- ments. The amino group of glycine, which has a pKa of 9.6, can exist either in the protonated form (-NH3 or as the free base (-NH2), because of the reversible equilibrium (a) In what pH range can glycine be used as an effective buffer due to its amino group? (b) In a 0.1 M solution of glycine at...
I have attached a titration of a mock amino acid with OH-. I have labeled the...
I have attached a titration of a mock amino acid with OH-. I
have labeled the different charge states of the amino acid as I,
II, III, IV. I have labeled different points on the titration curve
as A, B, ....G. I want you to tell me which form(s) of the species
I, II, III or IV predominates (is present at greatest
concentration) at each of the lettered points on the curve. I would
also like you to calculate the...
it's a bio-chem problem. "I have attached a titration of a mock amino acid with OH-....
it's a bio-chem problem.
"I have attached a titration of a mock amino acid with OH-. I
have labeled the different charge states of the amino acid as I,
II, III, IV. I have labeled different points on the titration curve
as A, B,...G. I want you to tell me which form(s) of the species
I,II,III,IV predominates (is present at greatest concentration) at
each of the lettered points on the curve. I would also like you to
calculate the PI...
it's a bio-chem problem. "I have attached a titration of a mock amino acid with OH-....
it's a bio-chem problem.
"I have attached a titration of a mock amino acid with OH-. I
have labeled the different charge states of the amino acid as I,
II, III, IV. I have labeled different points on the titration curve
as A, B,...G. I want you to tell me which form(s) of the species
I,II,III,IV predominates (is present at greatest concentration) at
each of the lettered points on the curve. I would also like you to
calculate the PI...
(18 pts) Answer True or False for each of the following questions (a) An amino acid...
(18 pts) Answer True or False for each of the following questions (a) An amino acid is in the zwitterionic form only if the pll is well below 7 (b) Salting out takes advantage of the fact that the solubility of proteins varies with concentration. (c) Proteins usually consists of amino acids of both L-isomers (d) Essentially all a-helices found in proteins are left-handed globular protein is thermodynamically the most stable structure. ( Isoclectric focusing can be used to separate...
Lecture 3 Identify amino-/carboxy termini, and R-group on amino acid What is chirality? Identify a carbon that is chiral (i.e., has 4 different groups attached) Chiral compounds rotate plane polarized light Memorize amino acid 1) structure, 2) classification (hydrophobic, aliphatic, aromatic, negatively charged, positively charged, polar uncharged) Be able to draw glycine (the generic amino acid) Given an amino acid structure and pKas of ionizable groups, be able to determine the charge at pH 1, pH 14, and pH 7...
of alanine has a pk of 9.87. What is the 153, The amino group charge on that amino group at pH 7.0 145. Which amino acid serves as the first amino acid at the hN terminus of a newly synthesized protein? (B) methionine (A) alanine 9.80. The side chain of that amino acid includes (A) an amine group (C) a carboxylic acid group. (D) an alcohol 154. A certain amino acid has a pl (or pH, isoelectric point) (D) threonine...
20. In most proteins this amino acid's side chain is found
clustered away from the aqueous exterior of the protein as a result
of which interaction?
a) Hydrophobic effect
b) Charge-charge (ionic)
c) Dipole-dipole
d) Van der Waals (dispersion)
A protein has a pI of 6.5. If I want to use an anion exchange
resin (there is a +ve charge on the resin) to bind the protein,
what pH could I perform the separation at?
a) pH 8
b) pH...
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...
20. Properties of a Buffer The amino acid glycine is often used as the main ingredient of a buffer in biochemical experi- ments. The amino group of glycine, which has a pKa of 9.6, can exist either in the protonated form (-NH3 or as the free base (-NH2), because of the reversible equilibrium (a) In what pH range can glycine be used as an effective buffer due to its amino group? (b) In a 0.1 M solution of glycine at...
I have attached a titration of a mock amino acid with OH-. I
have labeled the different charge states of the amino acid as I,
II, III, IV. I have labeled different points on the titration curve
as A, B, ....G. I want you to tell me which form(s) of the species
I, II, III or IV predominates (is present at greatest
concentration) at each of the lettered points on the curve. I would
also like you to calculate the...
it's a bio-chem problem.
"I have attached a titration of a mock amino acid with OH-. I
have labeled the different charge states of the amino acid as I,
II, III, IV. I have labeled different points on the titration curve
as A, B,...G. I want you to tell me which form(s) of the species
I,II,III,IV predominates (is present at greatest concentration) at
each of the lettered points on the curve. I would also like you to
calculate the PI...
it's a bio-chem problem.
"I have attached a titration of a mock amino acid with OH-. I
have labeled the different charge states of the amino acid as I,
II, III, IV. I have labeled different points on the titration curve
as A, B,...G. I want you to tell me which form(s) of the species
I,II,III,IV predominates (is present at greatest concentration) at
each of the lettered points on the curve. I would also like you to
calculate the PI...
(18 pts) Answer True or False for each of the following questions (a) An amino acid is in the zwitterionic form only if the pll is well below 7 (b) Salting out takes advantage of the fact that the solubility of proteins varies with concentration. (c) Proteins usually consists of amino acids of both L-isomers (d) Essentially all a-helices found in proteins are left-handed globular protein is thermodynamically the most stable structure. ( Isoclectric focusing can be used to separate...
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