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- 1. Use the info of this molecule as well as the attached addendum to demonstrate the flow of genetic information to protein sequence as described by the so-called “Central Dogma” . Clearly indicate the direction of your polynucleotide strands and peptide/protein. ATG GCA TGC AAT AGC TCA TGC 2. What would happen to the amino acid sequence if the underlined nucleotide (C) would change to an A?1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.1.Draw these phosphorylated structures as they would be connected in a polinucleotide (e.g.RNA) in the order A-B. / Show how they combine to form the polynuleotide (i.e. only the end product). Show at any one of these structures where the glycosidic bond occurs 2.Sanger sequencing revealed the sequence of an oligonucleotide to be: d-AGATGCCTGACT. Draw a diagram of the gel banding pattern post capillary electrophoresis i.e. where on the gel would the fragments feature
- 2 a. You are trying to purify protein C from a mixture of proteins noted in the above Table. If you had only one type of column to choose from, which one would allow you to purify protein C with the least number of contaminants? Size exclusion column Ion exchange column Affinity chromatography using glucose as the bait Affinity chromatography using NAD as the bait Please explain why you chose the column above based upon the properties of the column AND the proteins in the Table.The elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatography1) If there were two distantly protein, the best BLOSUM & PAM matrix is: ① BLOSUM 45 and PAM 250 ② BLOSUM 45 and PAM 1 ③ BLOSUM 80 and PAM 250 ④ BLOSUM 80 and PAM 1 Give typing answer with explanation and conclusion
- 6. THE FOLLOWING ARE DESCRIPTION OF NUCLEIC ACIDS. EXCEPT?A. MADE UP ALSO OF A NUCLEOSIDEB. COMPOSED OF CHAINS OF NUCLEOTIDESC. VERY LARGE, COMPLEX MOLECULESD. POLYMERS OF NON-REPEATING UNITS OF NUCLEOTIDES 7. ALL OF THE FOLLOWING ARE TRUE ABOUT DNA, EXCEPT?A. CONTAINS THE NITROGENOUS BASE URACILB. WITH ALPHA-HELICAL STRUCTUREC. INVOLVED IN PROTEIN SYNTHESISD. GENETIC CARRIER 8. WHICH OF THE FOLLOWING IS/ARE RESPONSIBLE FOR PROTEIN SYNTHESIS?A. T-RNAB. ALL OF THEMC. R-RNAD. M-RNA 9. WHICH OF THE FOLLOWING CAN AFFECT THE DNA STRUCTURE?A. ALL OF THEMB. UVC. BASE ANALOGUESD. IONIZING RADIATION 10. ALL OF THE FOLLOWING ARE PROTEIN ENZYMES, EXCEPT?A. PEPSINB. CHYMOTRYPSINC. PTYALIND. TRYPSIN1. What are the three general steps involved in isolation of proteins? Discuss or briefly describe the purpose of each step. 2. Suggest a simple procedure (or test) to verify if the final product is indeed casein.3)Consider the following sequence: 5' - AUGGCUACAGAUAGCUGGGGCUGAAAAAAAAAAAAAAA..3'Translated, the corresponding protein contains how many amino acids: a) 6 b) 7 c) 8 d) 13
- 6. a.) Which part (sugar, phosphate, or nitrogenous base) of the four types of nucleotides differ? b.) Based on the complementary base pairing rules we know that: A(denosine) pairs with _________ , and that G(uanine) pairs with _________.1. In the preparation of the standard curve for protein analysis, 50 mnBSA (bovine serum albumin) dissolved in H2O to a final volume of 5mL was used as stock solution. What is the weight of BSA in 0.1 mL ofstock solution? In 0.2 mL? The mentioned aliquots (#9) which were diluted with enough water to a final volume of 1 mL were assayed colorimetrically and yielded the following absorbance readings: mL stock mL H2O Absorbance0.2 0.8 0.1000.4 0.6 0.2000.6 0.4 0.3000.8 0.2 0.4001.0 0.0 0.500 i. Tabulate mg BSA vs. absorbance readingii. Draw the curve where mg BSA is on x-axis and absorbance ony-axis (use graphing paper).iii. Calculate the slope of the curveiv. If a sample solution has an absorbance of 0.332, determinemg protein of the sample.1. Explain why is it necessary for a protein to adopt specific tertiary and quaternary arrangements. 2.Explain the role of hydrogen bonding and disulfide bonds between R groups. 3. Explain the similarities and differences between rna and dna.