How do amino acid residues Asp102, His 57, and Ser 195 participate in peptide bond hydrolysis...
How do amino acid residues Asp102, His 57, and Ser 195 participate in peptide bond hydrolysis as catalyzed by chymotrypsin?
Homework Answers
Chymotrypsin is endopeptidase.It catalyzes the hydrolysis of the peptide bond on the C-side of amino acids that contain aromatic six-membered rings (Phe, Tyr, Trp) where Phe=phenylalanine, Tyr=tyrosine and Trp=tryptophan.
Endopeptidase such as chymotrypsin enzymes recognize the appropriate hydrolysis site by its shape and charge, and the cyclic structure of proline causes the hydrolysis site to have an unrecognizable three-dimensional shape.
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How do amino acid residues Asp102, His 57, and Ser 195
participate in peptide bond hydrolysis...
22. Label three amino acids- Asp, His and Ser and substrate peptide bond in the following...
22. Label three amino acids- Asp, His and Ser and substrate peptide bond in the following Chymotrypsin-catalyzed reaction mechanism and briefly describe their roles. Oxyanion hole Han Tetrahedral intermediate Acyl-enzyme Acyl-enzyme Oxyanion hole H- Tetrahedral intermediate Acyl-enzyme
B. Explain how two amino acid residues can form a peptide bond I was able to...
B. Explain how two amino acid residues can form a peptide bond I was able to get A) in this but I don't seem to understand this completely.
33, 48 Depicted below are a peptide substrate and the three catalytic residues within the chymotrypsin...
33, 48
Depicted below are a peptide substrate and the three catalytic residues within the chymotrypsin active site Note that the 2-dimensional geometry is only roughly shown. R1 represents a large hydrophobic amino acid and R represents other amino acids. The R groups of the catalytic triad of aspartate (Asp102), serine (Ser195), and histidine (His57) are shown. Select the atoms that act as nucleophiles and electrophiles in the acylation phase of the reaction Scroll down for more of this question...
An amino acid A, isolated from the acid-catalyzed hydrolysis of a peptide antibiotic, gave a positive...
An amino acid A, isolated from the acid-catalyzed hydrolysis of a peptide antibiotic, gave a positive ninhydrin test and had a specific optical rotation (HCl solution) of 37.5 mL/(g
Which of the statements about peptide bonds are true? D A tripeptide contains three amino acid...
Which of the statements about peptide bonds are true? D A tripeptide contains three amino acid residues. Peptide bonds are ester linkages. Peptide bond formation is a hydrolysis reaction. O Peptides are polymers of amino acids. Peptide bonds form from nucleophilic attack by an a-carboxyl carbon atom on an electron pair of an a-amino nitrogen atom of another amino acid.
3. Amino acid analysis of a peptide seven residues long gave: Asp, Leu, Lys,...
3. Amino acid analysis of a peptide seven residues long gave: Asp, Leu, Lys, Met, Phe, Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. Reaction with phenylisothiocyanate reagent yielded PTH-Phe c. Treatment with chymotrypsin yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free lysine. What is the...
The low barrier hydrogen bond formed between the buried Asp 102 and His 57 residues of...
The low barrier hydrogen bond formed between the buried Asp 102 and His 57 residues of the catalytic triad in the chymotrypsin mechanism serves to
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptid...
1.) Draw the structure of the amino acid Serine(ser), which has R=-CH2-OH. Label the alpha carbon. 2.) Draw the dipeptide that forms between serine and alanine. The dipeptide sequence is Ser-Ala. Label the peptide bond. 3.) How many amino acids residues are in a polypeptide containing 6 peptide bonds? How many peptide bonds are in a tripeptide 4.) Sketch a alpha-helix and a beta-sheet as best as you can. Label each.
Indicate which of the amino acid residues in the following peptide sequence contains a group that...
Indicate which of the amino acid residues in the following peptide sequence contains a group that has a negative charge for its most likely charge state at pH 10. Phe-Val-Pro-His-Trp-Asn-Cys-Thr-Asp Please explain in detail how you got the answer. thank you!
Indicate which of the amino acid residues in the following peptide sequence contains a group that...
Indicate which of the amino acid residues in the following peptide sequence contains a group that has a negative charge for its most likely charge state at pH 10. Glu-Cys-Tyr-Lys-Asp-Ile-Leu-His-Trp
22. Label three amino acids- Asp, His and Ser and substrate peptide bond in the following Chymotrypsin-catalyzed reaction mechanism and briefly describe their roles. Oxyanion hole Han Tetrahedral intermediate Acyl-enzyme Acyl-enzyme Oxyanion hole H- Tetrahedral intermediate Acyl-enzyme
33, 48
Depicted below are a peptide substrate and the three catalytic residues within the chymotrypsin active site Note that the 2-dimensional geometry is only roughly shown. R1 represents a large hydrophobic amino acid and R represents other amino acids. The R groups of the catalytic triad of aspartate (Asp102), serine (Ser195), and histidine (His57) are shown. Select the atoms that act as nucleophiles and electrophiles in the acylation phase of the reaction Scroll down for more of this question...
Which of the statements about peptide bonds are true? D A tripeptide contains three amino acid residues. Peptide bonds are ester linkages. Peptide bond formation is a hydrolysis reaction. O Peptides are polymers of amino acids. Peptide bonds form from nucleophilic attack by an a-carboxyl carbon atom on an electron pair of an a-amino nitrogen atom of another amino acid.
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