Homework Answers
Answer:
Enzymes cut their substrate after recognising a specific sequence of amino acid. Elastase and chymotrypsin recognise peptide bonds between hydrophobic or large amino acids, whereas arginine is hydrophilic. Hence, the first two options are incorrect.
On the other hand, Trypsin enzyme recognises arginine residues and cut peptide bond at its C terminal side.
Thus, correct choice should be: Trypsin.
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A peptide with the sequence "Glu-Ser-Arg-Asp-Lys" will be cut next to "Arg" by: chymotrypsin elastase trypsin...
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved...
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved by trypsin? b. What are the fragments, if it is cleaved by chymotrypsin? c. What are the fragments, if it is cleaved by pepsin?
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D....
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
please help!!! 19. A peptide is composed of the following amino acids: Ala, Arg. Glu, Gly,...
please help!!!
19. A peptide is composed of the following amino acids: Ala, Arg. Glu, Gly, Lys, Met, Phe, Ser, Tyn Given the following data deduce the sequence of the peptide. Trypsin digestion yielded two fragments with the following composition: Fragment 1: Ala, Arg, Glu, Met, Phe, Ser Fragment 2: Gly, Lys, Tyr Chymotrypsin digestion yielded three fragments with the listed compositions: Fragment 1: Ala, Gly, Lys, Phe Fragment 3: Arg, Glu, Met, Ser Cyanogen Bromide cleavage yielded two fragments...
3) Chymotrypsin acts on the following pentapeptide: Asp-Lys-Tyr-Gly-Ser. Which portion of the peptide will be the...
3) Chymotrypsin acts on the following pentapeptide: Asp-Lys-Tyr-Gly-Ser. Which portion of the peptide will be the first to leave the enzyme? A) Asp-Lys B Tyr-Gly-Ser C) Asp-Lys-Tyr D Gly-Ser
5) The binding pocket of trypsin, which normally cleaves after Arg and Lys, was modified to conve...
5) The binding pocket of trypsin, which normally cleaves after Arg and Lys, was modified to convert the key Asp to an Arg. Circle the dipeptide below would be the most likely to be cleaved by the modified trypsin. Draw the structure of the products of the reaction. Ile-Ser Val-Glu Glu-Val Lys-Val
5) The binding pocket of trypsin, which normally cleaves after Arg and Lys, was modified to convert the key Asp to an Arg. Circle the dipeptide below would...
Please answer thoroughly, will rate thumbs up. thanks Q1. Consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu. What...
Please answer thoroughly, will rate thumbs up. thanks Q1. Consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu. What is special about the arrangement of the amino acids in these sequences when incorporated into a Beta sheet? What prediction can you make about how this Beta sheet might be arranged in a cytoplasmic protein. Q2. Consider the following protein sequence as an Alpha-helix: Leu-Lys-Arg-Ile-Val-Asp-Ile-Leu-Ser-Arg-Leu-Phe-Lys-Val. What is special about the arrangement of the amino acids in these sequences when folded into alpha helix?
Which sequence is more soluble on water. a. Glu-Lys-Leu-Met-His b. Lys-Ser-Ser-Tyr-Glu c. Asp-Phe-Trp-Met-His d. His-Tyr-Ser-Ala-Glu e....
Which sequence is more soluble on water.
a. Glu-Lys-Leu-Met-His b. Lys-Ser-Ser-Tyr-Glu c. Asp-Phe-Trp-Met-His d. His-Tyr-Ser-Ala-Glu e. His-Ala-Cys-Gly-Glu o
Styles A decapeptide has the following amina acid composition: Arg. Asp, Gly, Leu, Lys, Met, Phe,...
Styles A decapeptide has the following amina acid composition: Arg. Asp, Gly, Leu, Lys, Met, Phe, Ser. Trp, and Val Reacting the native peptide with FDNB and then hydrolyzing released 2.4- dinitrophenylvaline. Brief incubation of the native peptide with carboxypeptidase yielded free Leu. Incubation with cyanogen bromide yielded two fragments: a tetrapeptide with composition Met, Phe, Ser, and Val, and a hexapeptide. The hexapeptide yielded 2.4- dinitrophenylglycine. Proteolytic cleavage by trypsin of the native peptide gave free Leu, a tripeptide,...
Predict the charge on the major species of the peptide Ile–Arg–Asp–Ala–Lys–Ser–Gln at pH 7.0
Predict the charge on the major species of the peptide Ile–Arg–Asp–Ala–Lys–Ser–Gln at pH 7.0
Can the peptide Ser-Glu-Pro-Ile-Met-Ala-Pro-Val-Glu-Tyr-Pro-Lys be hydrolyzed by chymotrypsin? our teacher indicates that it can, but i...
Can the peptide Ser-Glu-Pro-Ile-Met-Ala-Pro-Val-Glu-Tyr-Pro-Lys be hydrolyzed by chymotrypsin? our teacher indicates that it can, but i was under the impresion that if proline was the next amino acid, then the reaction would not go.
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved by trypsin? b. What are the fragments, if it is cleaved by chymotrypsin? c. What are the fragments, if it is cleaved by pepsin?
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
please help!!!
19. A peptide is composed of the following amino acids: Ala, Arg. Glu, Gly, Lys, Met, Phe, Ser, Tyn Given the following data deduce the sequence of the peptide. Trypsin digestion yielded two fragments with the following composition: Fragment 1: Ala, Arg, Glu, Met, Phe, Ser Fragment 2: Gly, Lys, Tyr Chymotrypsin digestion yielded three fragments with the listed compositions: Fragment 1: Ala, Gly, Lys, Phe Fragment 3: Arg, Glu, Met, Ser Cyanogen Bromide cleavage yielded two fragments...
3) Chymotrypsin acts on the following pentapeptide: Asp-Lys-Tyr-Gly-Ser. Which portion of the peptide will be the first to leave the enzyme? A) Asp-Lys B Tyr-Gly-Ser C) Asp-Lys-Tyr D Gly-Ser
5) The binding pocket of trypsin, which normally cleaves after Arg and Lys, was modified to convert the key Asp to an Arg. Circle the dipeptide below would be the most likely to be cleaved by the modified trypsin. Draw the structure of the products of the reaction. Ile-Ser Val-Glu Glu-Val Lys-Val
5) The binding pocket of trypsin, which normally cleaves after Arg and Lys, was modified to convert the key Asp to an Arg. Circle the dipeptide below would...
Which sequence is more soluble on water.
a. Glu-Lys-Leu-Met-His b. Lys-Ser-Ser-Tyr-Glu c. Asp-Phe-Trp-Met-His d. His-Tyr-Ser-Ala-Glu e. His-Ala-Cys-Gly-Glu o
Styles A decapeptide has the following amina acid composition: Arg. Asp, Gly, Leu, Lys, Met, Phe, Ser. Trp, and Val Reacting the native peptide with FDNB and then hydrolyzing released 2.4- dinitrophenylvaline. Brief incubation of the native peptide with carboxypeptidase yielded free Leu. Incubation with cyanogen bromide yielded two fragments: a tetrapeptide with composition Met, Phe, Ser, and Val, and a hexapeptide. The hexapeptide yielded 2.4- dinitrophenylglycine. Proteolytic cleavage by trypsin of the native peptide gave free Leu, a tripeptide,...
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