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- a. Identify the type of mutation shown below. b. How many amino acids are affected? c. What type of impact will this mutation have on the functionality of the protein? Second Letter UUU UUC UUA JUG UCu uCC UCA UCG UAU UAC UGU UOC Phe Tyr Cys Ser UAA Stop UGA Stop UAG Stop UGG Trp Leu cu cc Pro CUU COU CAU His CAC CUC CUA Leu Arg CCA Cca CGA CUG CAA Cin CAG AGU AGC AGA Arg AAU AUU AUC le AUA AUG Met ACO ACU ACC ACA Asn Ser AAC The MA AAG Lys AGG CAL KAC GUU Aep GUC Val CUA OCC Ala OCA GA Clu GAG Oly GOA GUG GGG Original DNA strand G AC 1. G. G. Mutated DNA strand GA Third lettera. The graph to the right displays the degree of helicity that was measured for a peptide as nine additional amino acids were sequentially added to the initial amino acid. Describe the reasons that the helicity curve takes the shape that it does as amino acids are added on to the small peptide.In relation to the peptide sequence that is presented. -Gly - Ser – Cys – Asp – Glu – Arg – Cys – Arg- ................ S_____________________S The correct option is A. Contains more negative than positive residues B. Contains only one charged alpha-aa C. The formation of the disulfide bridge is incorrect D. Hydrophilic and charged residues predominate
- Consider the following two peptides: I. N-Pro-Pro - Glu - Glu - Tyr - His - Cys - Ala - Glu - Gln - Lys - Leu - Ser - Ser - Phe-Leu- Thr - C II. N-Pro-Pro - Lys - Arg - Gly - Tyr - His - Gly - Glu - Asp - Glu - Asp - Glu - Ser - Gly-Phe- Tyr-C Give three reasons why_peptide I is more likely to form an alpha helix in aqueous solution at pH 7.0. Your reasons may include why_peptide Il is less likely to form an alpha helixA. One example of conjugated protein that contains the following Prosthetic groups: a. Iron Protein class, Example, b. Lipids Protein class, Example, c. Phosphate group Protein class, Example, d. Carbohydrate Protein class, Example, е. Heme Protein class, Example,Draw the bond-line structure of the given peptides. 1. Ser-Asp 2. Glu-Gln 3. Arg-His 4. Ala-Val-Ser 5. Glu-Gln-Gly 6. Cys-Gly-Asn
- B. Enumerate all the possible DNA nucleotide base sequence for the amino acids given. 4. Met – Leu – Ala - Gly- Glu - Gly- Gln- Glu- Ala - Ala - Pro - LeuTranslate the given amino acid sequence into one-letter code. Glu-Leu-Val-Ile-Ser-Ile-Ser-Leu-Ile-Val-Ile-Asn-Gly-Ile-Asn-Ala-Thr-Leu-Ala-Asn-Thr-Ala Translated code: X Incorrecta. Identify the type of mutation shown below. b. How many amino acids are affected? c. What type of impact will this mutation have on the functionality of the protein?
- Subjecting this peptide to one cycle of the Edman degradation would result in L-M-F-V-W-E-Q-A-P-S-P Leucine OA. O B. Proline oc Leucine phenylthiohydantoin OD. Proline phenylthiohydantoin None of the above OE.Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsinConsider the peptide L-E-T-S-P-R-A-Y Which amino acid(s) is/are basic? A. Y B. P C. R D. L E. T F. S C. A H. E