Predict the charge on the major species of the peptide Ile-Lys-Asp-Arg-Ser-Gln at pH 7.0
Please explain if you can. Thanks
Predict the charge on the major species of the peptide Ile-Lys-Asp-Arg-Ser-Gln at pH 7.0 Please explain...
Predict the charge on the major species of the peptide Ile–Arg–Asp–Ala–Lys–Ser–Gln at pH 7.0
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...
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?
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 of these protein sequences is most likely to span a cell membrane? Gly-Asp-Val-Ala-Gly-Arg-Gly-Asn-Gly-Lys-Lys-Pro-Ser-Ser-Val-Arg-Ala-Leu-Ser Ile-Val-Leu-Pro-Ile-Val-Leu-Leu-Val-Phe-Leu-Cys-Leu-Gly-Val-Phe-Leu-Leu-Trp Lys-Asn-Trp-Arg-Leu-Lys-Asn-Ile-Asn-ser-Ile-Asn-Phe-Asp-Asn-Pro-Val-Tyr-Gln A. 773 B. 792 C. 811
A peptide with the sequence "Glu-Ser-Arg-Asp-Lys" will be cut next to "Arg" by: chymotrypsin elastase trypsin D. All of the above. E None of the above.
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,...
On your internship, you visit the Mass Spectrometry Lab. Mass spectrometry can identify short peptide fragments based on their molecular weights. Your fellow intern Jerry has neglected to label his tubes of amyloid beta peptide 42 after digesting them with some proteases that we learned about in Module 6: pepsin, trypsin, and chymotrypsin. Help him figure out what protease is in each tube. Jerry’s supervisor has the fragments listed in the same order as the original peptide primary sequence, which...
Consider the following amino acid sequence, found as part of a larger protein: Pro-Gly-Asp-Val-Gln-Phe-Asp-Ile-Arg-Ala-Asp-Gly What kind of structure do you expect this peptide segment be a part of? Where on the protein is this likely to occur?
Sketch the structure of the tetrapeptide Ser-Phe-Asp-Lys. Clearly show the R groups, all the peptide bonds, the peptide planes, the N-terminus, the C-terminus, and approximate charges on all ionic groups at a pH of 7.0.