Deduce the sequence of a heptapeptide that contains the amino acids Met, Gln, Phe, Leu, Cys, Val, and Arg, from the following experimental data. Edman degradation cleaves Cys from the heptapeptide, and carboxypeptidase forms Gln and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Gln, Cys, Phe, and the tripeptides Leu-Met-Val and Met-Val-Arg.
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Deduce the sequence of a heptapeptide that contains the amino
acids Met, Gln, Phe, Leu, Cys,...
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase...
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Cys (octapeptide), Cys (A), Gln (B), Cys (C), Glu(D). Partial hydrolysis of tetrapeptide B forms Gln-Thr in addition to other products....
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase...
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Cys (octapeptide), Cys (A), Gln (B), Cys (C), Glu(D). Partial hydrolysis of tetrapeptide B forms Gln-Thr in addition to other products....
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,...
Be sure to answer all parts. An octapeptide contains the following amino acids: Ala, Pro, Gly,...
Be sure to answer all parts. An octapeptide contains the following amino acids: Ala, Pro, Gly, Asp, Trp, Lys, Leu, Met. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Gly (octapeptide),Gly (A),Met (B), Gly (C), Leu(D).Partial hydrolysis of tetrapeptide B forms Met-Pro in addition...
biochemistry please show your work 2. A mutant form of polypeptide hormone angiotensin II has the...
biochemistry please show your work
2. A mutant form of polypeptide hormone angiotensin II has the amino acid composition: Ile, Arg, Met, Leu, Phe, Asp, Tyr, and Val. The following observations are made: 1) Treatment with trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. 2) Cyanogen bromide yields a dipeptide containing Phe and Leu and a hexapeptide containing all the rest. 3) Chymotrypsin cleaves the hormone into two tetrapeptides of composition: Val, Tyr,...
Please be specific about the solution and thank you O points) Deduce the sequence of a...
Please be specific about the solution and thank
you
O points) Deduce the sequence of a pentapeptide that contains the amino acids Ala, Lys, Gly, Ser, and Tyr, from the following experimental data. Edman degradation cleaves Gly from the pentapeptide, and trypsin treatment gives Ala and a tetrapeptide. Treatment of the pentapeptide with chymotrypsin forms a dipeptide and a tripeptide. Partial hydrolysis forms Gly, Ser, and the tripeptide Tyr-Lys-Ala.
Use the given experimental data to deduce the sequence of an octapeptide that contains the amino...
Use the given experimental data to deduce the sequence of an octapeptide that contains the amino acids His, Ala (2 equiv), Val (2 equiv), Ser, Gly, and Pro. Edman degradation cleaves Ala from the octapeptide, and carboxypeptidase forms Gly and a heptapeptide. Partial hydrolysis forms the following fragments: Pro-Val-Gly, His-Val-Pro, Ala, and Ala-Ser-His-Val.
4. Complete hydrolysis of a heptapeptide T gave the following amino acids: 2Ảla, Glu, Leu, Lys,...
4. Complete hydrolysis of a heptapeptide T gave the following amino acids: 2Ảla, Glu, Leu, Lys, Phe, Val Deduce the amino acid sequence of T from the following data: i. Sequential treatment of T with 2,4-dinitrofluorobenzene (DNFB) and incomplete hydrolysis gave DNP-Val followed by DNP-Leu. Hydrolysis of T with carboxypeptidase gave Ala followed by Glu. Partial enzymatic hydrolysis of T gave a dipeptide and a tripeptide V. U with DNFB and hydrolysis gave DNP-Leu followed by DNP-Lys. 2. Complete hydrolysis...
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?
Need help with #2 Clearly provide the 3-letter symbol for the correct sequence of cach amino...
Need help with #2
Clearly provide the 3-letter symbol for the correct sequence of cach amino acid in each of listings of the amino acids in the peptide or in any fragments are simply listed in alphabetical order. A subscriptive the number of that amino acid. Use parentheses to incorporate the unknown amino acids after each treatment 1. A five amino acid peptide contains: Arg. Glu, His, Phe, and Ser This peptide yields the following results when broken down into...
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,...
Be sure to answer all parts. An octapeptide contains the following amino acids: Ala, Pro, Gly, Asp, Trp, Lys, Leu, Met. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Gly (octapeptide),Gly (A),Met (B), Gly (C), Leu(D).Partial hydrolysis of tetrapeptide B forms Met-Pro in addition...
biochemistry please show your work
2. A mutant form of polypeptide hormone angiotensin II has the amino acid composition: Ile, Arg, Met, Leu, Phe, Asp, Tyr, and Val. The following observations are made: 1) Treatment with trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. 2) Cyanogen bromide yields a dipeptide containing Phe and Leu and a hexapeptide containing all the rest. 3) Chymotrypsin cleaves the hormone into two tetrapeptides of composition: Val, Tyr,...
Please be specific about the solution and thank
you
O points) Deduce the sequence of a pentapeptide that contains the amino acids Ala, Lys, Gly, Ser, and Tyr, from the following experimental data. Edman degradation cleaves Gly from the pentapeptide, and trypsin treatment gives Ala and a tetrapeptide. Treatment of the pentapeptide with chymotrypsin forms a dipeptide and a tripeptide. Partial hydrolysis forms Gly, Ser, and the tripeptide Tyr-Lys-Ala.
4. Complete hydrolysis of a heptapeptide T gave the following amino acids: 2Ảla, Glu, Leu, Lys, Phe, Val Deduce the amino acid sequence of T from the following data: i. Sequential treatment of T with 2,4-dinitrofluorobenzene (DNFB) and incomplete hydrolysis gave DNP-Val followed by DNP-Leu. Hydrolysis of T with carboxypeptidase gave Ala followed by Glu. Partial enzymatic hydrolysis of T gave a dipeptide and a tripeptide V. U with DNFB and hydrolysis gave DNP-Leu followed by DNP-Lys. 2. Complete hydrolysis...
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?
Need help with #2
Clearly provide the 3-letter symbol for the correct sequence of cach amino acid in each of listings of the amino acids in the peptide or in any fragments are simply listed in alphabetical order. A subscriptive the number of that amino acid. Use parentheses to incorporate the unknown amino acids after each treatment 1. A five amino acid peptide contains: Arg. Glu, His, Phe, and Ser This peptide yields the following results when broken down into...
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