Draw the structure of Tetrapeptide Phe Thr Met His
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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....
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?
Write down the mRNA sequence for: start-val-ala-thr-thr-leu-tyr-cys-gly-arg-stop start-lys-asn-gly-phe-his-thr-arg-pro-gln-stop start-met-thr-asn-lys-pro-gln-ser-leu-arg-stop
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe and Gly-Arg-Met 3) Ala-Val-Trp-Lys-Phe-Gly and Arg-Met - Ala-Val-Trp-Lys and Phe-Gly-Arg and Met ) Ala-Val-Trp-Lys and Phe and Gly-Arg and Met ) Ala-Val-Trp and Lys-Phe-Gly and Arg-Met Bradykinin is a nonapeptide, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. In addition to one mole of Arg, what peptides are present after hydrolysis of bradykinin with chymotrypsin? A) Arg-Pro-Pro and Gly-Phe and Ser-Pro-Phe B) Pro-Pro-Gly and Phe-Ser-Pro-Phe-Arg C) Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe ?) Arg-Pro-Pro-Gly-Phe-Ser...
. Draw structures of Phe-Gly and Ser-Met dipeptides Phe-Gly Ser-Met
The sequence Leu-Val-Leu-Glu-Phe-Met-Ile-Thr is most compatible with which of the following protein structures? A) coiled coil B) solitary transmembrane helix C) curved transmembrane beta sheet D) Helix in a multihelix transmembrane channel
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,...
[B] Draw structure of the pentapeptide Met-Phe-Leu-Pro -Trp (10 Points)
Write the structure of the tripeptide Thr-Phe-Tyr. (Draw only the unionized condensed structural representation of the product. Omit any lone pairs, radical electrons, atomic charges, or stereochemical markers from your answer.)