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DIPEA is tertiary amine used as base, but poor nucleophile. central N atom is surrounded by the two isopropyl groups and has only space to accept the hydrogen atom.

Coupling of peptides occurs at slightly basic pH. HBTU converts Fmoc amino acid into active ester in presence of one equivalent of base. For this purpose DIPEA is routinely used.

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How are peptide bonds formed during protein synthesis?

During protein synthesis, peptide bonds are formed through a process called condensation reaction. This reaction occurs between the carboxyl group of one amino acid and the amino group of another amino acid, resulting in the formation of a peptide bond and the release of a water molecule. This process is catalyzed by enzymes called ribosomes.


What role does peptide bond play in protein synthesis?

Although rRNA is paramount in the process of translation, protein factors also are required for the efficient synthesis of a protein. Protein factors participate in the initiation, elongation, and termination of protein synthesis. P-loop NTPases of the G-protein family play particularly important roles. Recall that these proteins serve as molecular switches as they cycle between a GTP-bound form and a GDP-bound form.


What is the bonding between the two amino acids in the ribosome called?

The bonding between two amino acids in the ribosome is called a peptide bond. This bond forms during protein synthesis when the carboxyl group of one amino acid reacts with the amino group of another amino acid, resulting in the formation of a peptide linkage.


How is BPC 157 made and what is the process involved in its production?

BPC 157 is a synthetic peptide that is made in a laboratory through a process called solid-phase peptide synthesis. This involves combining amino acids in a specific sequence to create the peptide. The process typically includes steps such as activation of amino acids, coupling them together, and purification of the final product.


What is the function of peptidyl transferase during translation?

Peptidyl transferase is an enzyme responsible for catalyzing the formation of peptide bonds between amino acids during translation. It is located in the ribosome and plays a crucial role in protein synthesis by facilitating the elongation of the polypeptide chain.

Related Questions

What does protein synthesis consist of?

peptide


In protein synthesis a nucleus forms peptide bonds?

In protein synthesis, peptide bonds are formed in the ribosome, not in the nucleus. The nucleus is responsible for housing the DNA and transcribing it into messenger RNA (mRNA) for protein synthesis to occur in the ribosome.


What is the three-letter code for lysine and what is its role in protein synthesis?

The three-letter code for lysine is Lys. Lysine is an essential amino acid that plays a key role in protein synthesis by helping to form peptide bonds between amino acids in the growing protein chain.


What is peptide transferase?

Peptidyl transferase is the enzyme that catalyzes the formation of peptide bonds between amino acids during translation of protein synthesis.


What is the three-letter code for the amino acid glutamine and what role does it play in protein synthesis?

The three-letter code for the amino acid glutamine is Gln. Glutamine plays a crucial role in protein synthesis as it is involved in providing nitrogen for the formation of peptide bonds between amino acids, which are essential for building proteins.


What kind of a reaction forms a peptide bond?

dehydration synthesis


What process produces peptide bonds?

A dehydration synthesis reaction forms peptide bonds between amino acids by removing a water molecule. In this process, the carboxyl group of one amino acid reacts with the amine group of another amino acid, resulting in the formation of a peptide bond and a dipeptide molecule.


Which type of reaction are essentially opposites of one another?

Decomposition and synthesis, peptide bonding and hydrolysis, etc.


What has the author Horst Kleinkauf written?

Horst Kleinkauf has written: 'Biochemistry of Peptide Antibiotics' -- subject(s): Biotechnology, Beta lactam antibiotics, Synthesis, Microbial peptides, Peptide antibiotics


How are peptide bonds formed during protein synthesis?

During protein synthesis, peptide bonds are formed through a process called condensation reaction. This reaction occurs between the carboxyl group of one amino acid and the amino group of another amino acid, resulting in the formation of a peptide bond and the release of a water molecule. This process is catalyzed by enzymes called ribosomes.


Is a peptide bond a covalent bond?

Yes, a peptide bond is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another amino acid during protein synthesis.


WHAT IS PEPTIDE SYNTHESIS?

The Peptides are naturally occurring biological molecules made up of short chains of amino acid residues carry secondary structure of protein. In typical peptides, when 30-40 amino acids are linked together by Peptides bonds, several water molecules are released. The shortest peptides are dipeptides, consisting of 2 amino acids joined by a single peptide bond, followed by tripeptides, tetrapeptides, oligopeptides and polypeptides etc. Therefore, a polypeptide is a long, continuous, unbranched peptide chain contains approximately 50 or fewer amino acids distinguished from proteins on the basis of size, an arbitrary benchmark used to understand the difference between the two.