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4. Complete hydrolysis of a heptapeptide T gave the following amino acids: 2Ảla, Glu, Leu, Lys,...
1. Partial hydrolysis of lysozyme yielded an octapeptide that was later identified as the N-terminal segment of the protein. From the following information, determine the sequence of this octapeptide. a. The following amino acids were identified after complete hydrolysis of the octapeptide: Arginine (Arg) Glycine (Gly) Phenylalanine (Phe) Cysteine (Cys) Leucine (Leu) Valine (Val) Glutamic Acid (Glu) Lysine (Lys) b. Treatment of the octapeptide with dinitroflurobenzene (Sanger reagent) followed by complete hydrolysis gave lysine (Lys) labeled with two dinitrophenyl (DNP) groups. c. Treatment of the octapeptide with trypsin gave lysine...
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. Be sure to answer...
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...
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,...
Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser. Problem 24-44 ConstantsI Periodic Table Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, lle, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala and the C terminus is lle. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that...
. Insulin (below) is treated with dansyl chloride followed by its complete acidic hydrolysis. Which of the following dansylated amino acids you expect to observe? A chain Gly-Ile-Val-Glu-Gln-Cys-Cys- Ala-Ser-Val - Cys-Ser-Leu- Tyr-Gln-Leu-Glu-Asn - Tyr-Cys- Asn 10 15 21 B chain Phe-Val - Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu - Ala-Leu-Tyr-Leu-Val-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys - Ala 10 20 25 30 15
Question 5 Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...
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 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....
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...