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- SDS coats proteins with a: A) Positive Charge B) Negative ChargeDeduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, SerEach of the ff. involves a disorder in the function of an organelle or other cell structure. Identify the cell organelle or cell structure involved and indicate whether it is likely to be underactive or active. a) A baby is placed on a low phenylalanine diet as his newborn screening results revealed that he inherited phenylketonuria. b) A girl suddenly felt weak and manifested cyanide poisoning symptoms after ingesting undercooked cassava which contains cyanoglycosides. c) A man develops pleiomorphic liposarcoma (rare cancer). The cause of the problem is a hard mass of cells in his right inner thigh that rapidly increased in size in a matter of 2 months. d) A male chef learns that he is infertile because his sperm are non-motile. Helping tags: biology, cell biology, cell structure, cell organelle
- Rationalize the following observations.(a) Serine is the amino acid residue that can be replaced with theleast effect on protein structure and function.(b) Replacement of tryptophan causes the greatest effect on protein structure and function.(c) Replacements such as Lys -> Arg and Leu -> Ile usually havevery little effect on protein structure and function.The macrolide below is a bacteria produced toxin. The primer was acetyl-Co-A. Three possible extenders are also shown A) malonate-Co-A B) methylmalonate-Co-A and C) ethylmalonate- Со-А. Indicate which extenders were used using this format: XA yB zC Meaning x molecules of A, y molecules of B and z molecules of C он COA CH3 А А но CH3 CoA В но ČH3 H3C C C HO но COA CH3 Enter Your Answer:5 25) Although the UV280 extinction coefficient of BSA is well known, why was the BCA assay employed to measure protein concentration of the folate labeled BSA? Please provide an explanation. (C) Would the use of reducing agents have an affect on the tertiary structure of BSA—please explain your answer (you will need to investigate the structure of BSA beyond this article)?
- 10. (a) Provide the scheme of Merrifield peptide synthesis with suitable example. (b) Describe the mechanism of action of the enzyme lysozyme.Which of the following is an anomer of B-D-gulopyranose? O O го ОН H ОН H ОН H H ОН CH₂OH -II- H H ОН ОН CH2OH H ОН ОН CH2OH О 0. H CH2OH то Н H H ОН H H - о H ОН ОН H ОН H ОН ОН H О ОН ОН H NDetermine the Primary amino acid sequence of an Octapeptide Composition · Tyr , Arg,Pro, Lys ,Lys ,Met ,Trp,Phe N terminal 1 2 3 4 5 6 7 8 C terminal 1) Treatment with an Edman reagent gives a PTH-AA that shows a Yellow color with Ninhydrin. 2) Trypsin digestion of the Octapeptide gives tetepeptide, dipeptide, free Arg ,free Trp. 3)CNBr = pentapeptide and tripeptide. 4) chymotrysin - tetapeptide and two dipeptiele. The tetrapeptide contains an amino acid with an OH group in the side chain.
- 23. In the structure below, the shaded areas H Ca Ca. H a) SDS gel electrophoresis b) mass spectrometry c) Edman degradation d) size exclusion chromatography Ca a) are unable to freely rotate around the C-N bond b) represent resonance structures c) represent a partial double bond between C and N d) all of the above Ca. 24. Which of the following protein separation techniques allows for the recovery of protein?1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. inPredict the fragments that will be generated from the treatment of the following peptide with: a) trypsin; b) chymotrypsin; c) and S. aureus V8 protease: Gly-Ala-Trp-Arg-Asp-Ala-Lys-Glu-Phe-Gly-Gln