Explain why synthesis of a dipeptide from two individual amino acids is energetically unfavorable. Explain how...
Explain why synthesis of a dipeptide from two individual amino acids is energetically unfavorable. Explain how this unfavorable synthesis may occur in biological systems.
Homework Answers
Di-peptide formation is an energetically unfavorable. Di-peptide formation involves joining of two amino acids via amide linkage.
Formation of amide linkage is an example of condensation reaction which involves the removal of water molecules from alpha carboxyl group of one amino acid and alpha carboxyl group of another amino acid. Mechanistically, alpha amino group acts as a nucleophile and displaces the hydroxyl group of alpha carboxyl group.
Amino group is a good nucleophile. Nonetheless, hydroxyl group is a poor leaving group and hence difficult to remove. Therefore, synthesis of peptide bond formation is not a favorable reaction.
Thus, cell overcomes this problem by chemical modification of carboxyl group. Chemical modification of carboxyl group leads to its activation and ease the removal of hydroxyl group in an energetically favorable manner.
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Explain why synthesis of a dipeptide from two individual amino
acids is energetically unfavorable. Explain how...
True or False: The form of dipeptide aspartylserine (Asp-Ser) obtained from two amino acids are drawn...
True or False: The form of
dipeptide aspartylserine (Asp-Ser) obtained from two amino acids
are drawn as:
The form of dipeptide aspartylserine (Asp-Ser) obtained from two amino acids are drawn as:
The synthesis of protein or polypeptides from individual amino acids would seem to cause a decrease...
The synthesis of protein or polypeptides from individual amino acids would seem to cause a decrease in entropy and require some sort of energy input. How is the energy supplied for protein synthesis?
How many unique dipeptides could be made from two different amino acids? Both amino acids do...
How many unique dipeptides could be made from two different amino acids? Both amino acids do not have to be used in each dipeptide.
On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together....
On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together. If the two amino acids are valine and threonine, predict the overall charge of the dipeptide at pH 7. Do not forget to consider the amino (N-terminal) and carboxy (C-terminal) of the dipeptide, as well as the R groups. Select one: a. +2 b. -2 c. 0 d. -1 e. +1
2. what is the configuration of almost all naturally occurring amino acids at the a (alpha)...
2. what is the configuration of almost all naturally occurring amino acids at the a (alpha) carbon 3. why is an alpha amino acid such as alanine more acidic than a regular carboxyllic acid 4. strecker synthesis Formation dl-phenylalanine 5. outline the steps to synthesize the simple dipeptide AL (think about two amino acids that begin with an A and an L) 6. give the structure and name of the nucleosides in dna and rna 7. give the structure of...
Question 4 30 pts How can a metabolic pathway contain an energetically unfavorable reaction yet still...
Question 4 30 pts How can a metabolic pathway contain an energetically unfavorable reaction yet still occur? The free-energy changes of the individual steps in a pathway are summed to determine the overall free-energy change. [Choose] TRUE FALSE [Choose] A step in a pathway that is energetically unfavorable can be driven by coupling it to a thermodynamically favorable reaction. [Choose ] At equilibrium, very few "energetically unfavored" products might be present - but if these unfavored products are then being...
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...
Why is it significant that all biological systems use L-amino acids and D-sugars?
Why is it significant that all biological systems use L-amino acids and D-sugars?
11/. Explain how this synthesis of amino acids, starting with natural proline, works. Explain the stereoselectivity...
11/. Explain how this synthesis of amino acids, starting with natural proline, works. Explain the stereoselectivity of each step after the first. NH CO, Me CO2H - NH, KHÓ CFCO,H CF,CO2H COLH HOC NH2 HR HT
1.) Why is it that amino acids in proteins are called a-amino acids? 2.) explain alpha,...
1.) Why is it that amino acids in proteins are called a-amino acids? 2.) explain alpha, amino, and acid . Please answer questions 1&2 !
True or False: The form of
dipeptide aspartylserine (Asp-Ser) obtained from two amino acids
are drawn as:
The form of dipeptide aspartylserine (Asp-Ser) obtained from two amino acids are drawn as:
How many unique dipeptides could be made from two different amino acids? Both amino acids do not have to be used in each dipeptide.
2. what is the configuration of almost all naturally occurring amino acids at the a (alpha) carbon 3. why is an alpha amino acid such as alanine more acidic than a regular carboxyllic acid 4. strecker synthesis Formation dl-phenylalanine 5. outline the steps to synthesize the simple dipeptide AL (think about two amino acids that begin with an A and an L) 6. give the structure and name of the nucleosides in dna and rna 7. give the structure of...
Question 4 30 pts How can a metabolic pathway contain an energetically unfavorable reaction yet still occur? The free-energy changes of the individual steps in a pathway are summed to determine the overall free-energy change. [Choose] TRUE FALSE [Choose] A step in a pathway that is energetically unfavorable can be driven by coupling it to a thermodynamically favorable reaction. [Choose ] At equilibrium, very few "energetically unfavored" products might be present - but if these unfavored products are then being...
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...
11/. Explain how this synthesis of amino acids, starting with natural proline, works. Explain the stereoselectivity of each step after the first. NH CO, Me CO2H - NH, KHÓ CFCO,H CF,CO2H COLH HOC NH2 HR HT
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