What is the overall charge for this pentapeptide Leu-Met-Lys-Arg at pH 7? will it bind to an anion exchange column at this pH?
please explain the process
thank you
Since at pH=7, overall net charge on the peptide is +2. it is positively charged.
so It will not bind to an anion exchange column because it is not negatively charged at pH=7.
To bind an anion exchange column molecule must be negatively charged.
What is the overall charge for this pentapeptide Leu-Met-Lys-Arg at pH 7? will it bind to...
Draw the Lewis structure of the pentapeptide Met-Glu-Leu-His-Lys as it will exist at the following pH's РH 2.5 a. b. рH 7.0 pH 10.0 с. d. What is the isoelectric point for this peptide? Draw the Lewis structure of the pentapeptide Met-Glu-Leu-His-Lys as it will exist at the following pH's РH 2.5 a. b. рH 7.0 pH 10.0 с. d. What is the isoelectric point for this peptide?
Please explain. 8. What will be the overall charge of the following peptide in the following pH values? (10 points) Arg Glu Glu Lys Asn Trp Met Tyr Arg Leu Lys OH Overall 7 14 4
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,...
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?
The overall charge of the polypeptide His-Tyr-Lys-Met-Ile-Glu at pH 6.9 is __? Please explain how you got the answer.
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...
What is the approximate net charge of the following pentapeptide at pH 10? Arg-Gln-Cys-His-Ala What is the Isoelectric point (pI) of the peptide given above? Use the pKa values given here when needed: Side group/ amino acid pKa Asp 3.9 Glu 4.1 HIs 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 C-term 3.5 N-term 9.0
3. A protein contains the following amino acids: O ALA 4 GLN 1 LEU 3 ARG 4 GLU 4 LYS 4 ASN 5 GLY O MET 1 ASP 1 HIS 2 PHE 4 ILE 4 PRO 8 SER 5 THR 1 TRP 2 TYR 2 VAL BGYS. a) What is its net charge at pH 1? b) What is its net charge at PH 13? c) Calculate the pl. 4. In what order would the amino acids GLU, LYS, and...
please explain each question thoroughly. thanks Question 3: Arg-Cys-Met-Ala-Cys-Gly-Arg-Pro-Asn-Tyr-Leu-Trp-Ala-Ile-His-Phe-Ser-Cys-Lys a. What would happen if this peptide were to be incubated with dinitrofluorobenzene (FDNB) followed by 6M HCl hydrolysis at 1100C for 24 hrs. What labeled product(s) would be detected? Consider the following pepide: What would happen if the peptide were treated with CNBr? What would the products be? Why? b. What would happen if the peptide were treated with chymotrypsin? What would the c. products be? Why? Arg-Cys-Met-Ala-Cys-Gly-Arg-Pro-Asn-Tyr, Leu-Trp, Ala-Ile-His-Phe,...
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?